Skip to main content
NCBI home page
Microbiological Reviews logoLink to Microbiological Reviews
. 1988 Jun;52(2):190–232. doi: 10.1128/mr.52.2.190-232.1988

Nitrate respiration in relation to facultative metabolism in enterobacteria.

V Stewart
PMCID: PMC373136  PMID: 3045516

Full text

PDF
190

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. 't Riet J van, Stouthamer A. H., Planta R. J. Regulation of nitrate assimilation and nitrate respiration in Aerobacter aerogenes. J Bacteriol. 1968 Nov;96(5):1455–1464. doi: 10.1128/jb.96.5.1455-1464.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Abou-Jaoudé A., Chippaux M., Pascal M. C. Formate-nitrite reduction in Escherchia coli K12. 1. Physiological study of the system. Eur J Biochem. 1979 Apr 2;95(2):309–314. doi: 10.1111/j.1432-1033.1979.tb12966.x. [DOI] [PubMed] [Google Scholar]
  3. Abou-Jaoudé A., Pascal M. C., Chippaux M. Formate-nitrite reduction in Escherichia coli K12. 2. Identification of components involved in the electron transfer. Eur J Biochem. 1979 Apr 2;95(2):315–321. doi: 10.1111/j.1432-1033.1979.tb12967.x. [DOI] [PubMed] [Google Scholar]
  4. Abraham P. R., Wientjes F. B., Nanninga N., Van't Riet J. Part of respiratory nitrate reductase of Klebsiella aerogenes is intimately associated with the peptidoglycan. J Bacteriol. 1987 Feb;169(2):849–855. doi: 10.1128/jb.169.2.849-855.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Adams M. W., Mortenson L. E. The effect of cyanide and ferricyanide on the activity of the dissimilatory nitrate reductase of Escherichia coli. J Biol Chem. 1982 Feb 25;257(4):1791–1799. [PubMed] [Google Scholar]
  6. Adhya S., Cleary P., Campbell A. A deletion analysis of prophage lambda and adjacent genetic regions. Proc Natl Acad Sci U S A. 1968 Nov;61(3):956–962. doi: 10.1073/pnas.61.3.956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Aliabadi Z., Warren F., Mya S., Foster J. W. Oxygen-regulated stimulons of Salmonella typhimurium identified by Mu d(Ap lac) operon fusions. J Bacteriol. 1986 Mar;165(3):780–786. doi: 10.1128/jb.165.3.780-786.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Alper M. D., Ames B. N. Positive selection of mutants with deletions of the gal-chl region of the Salmonella chromosome as a screening procedure for mutagens that cause deletions. J Bacteriol. 1975 Jan;121(1):259–266. doi: 10.1128/jb.121.1.259-266.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Amarasingham C. R., Davis B. D. Regulation of alpha-ketoglutarate dehydrogenase formation in Escherichia coli. J Biol Chem. 1965 Sep;240(9):3664–3668. [PubMed] [Google Scholar]
  10. Ames G. F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem. 1986;55:397–425. doi: 10.1146/annurev.bi.55.070186.002145. [DOI] [PubMed] [Google Scholar]
  11. Amy N. K., Rajagopalan K. V. Characterization of molybdenum cofactor from Escherichia coli. J Bacteriol. 1979 Oct;140(1):114–124. doi: 10.1128/jb.140.1.114-124.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Au D. C., Green G. N., Gennis R. B. Role of quinones in the branch of the Escherichia coli respiratory chain that terminates in cytochrome o. J Bacteriol. 1984 Jan;157(1):122–125. doi: 10.1128/jb.157.1.122-125.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Au D. C., Lorence R. M., Gennis R. B. Isolation and characterization of an Escherichia coli mutant lacking the cytochrome o terminal oxidase. J Bacteriol. 1985 Jan;161(1):123–127. doi: 10.1128/jb.161.1.123-127.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Azoulay E., Pommier J., Riviere C. Membrane reconstitution in chl-r mutants of Escherichia coli K 12. IX. Part played by phospholipids in the complementation process. Biochim Biophys Acta. 1975 May 6;389(2):236–250. doi: 10.1016/0005-2736(75)90318-1. [DOI] [PubMed] [Google Scholar]
  15. Azoulay E., Puig J., Couchoud-Beaumont P. Etude des mutants chlorate-résistants chez Escherichia coli K 12. I. Reconstitution in vitro de l'activité nitrate-réductase particulaire chez Escherichia coli K 12. Biochim Biophys Acta. 1969 Feb 11;171(2):238–252. doi: 10.1016/0005-2744(69)90157-0. [DOI] [PubMed] [Google Scholar]
  16. Azoulay E., Puig J., Pichinoty F. Alteration of respiratory particles by mutation in Escherichia coli K 12. Biochem Biophys Res Commun. 1967 Apr 20;27(2):270–274. doi: 10.1016/s0006-291x(67)80073-1. [DOI] [PubMed] [Google Scholar]
  17. Ballantine S. P., Boxer D. H. Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli. Eur J Biochem. 1986 Apr 15;156(2):277–284. doi: 10.1111/j.1432-1033.1986.tb09578.x. [DOI] [PubMed] [Google Scholar]
  18. Ballantine S. P., Boxer D. H. Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. J Bacteriol. 1985 Aug;163(2):454–459. doi: 10.1128/jb.163.2.454-459.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Barrett E. L., Clark M. A. Tetrathionate reduction and production of hydrogen sulfide from thiosulfate. Microbiol Rev. 1987 Jun;51(2):192–205. doi: 10.1128/mr.51.2.192-205.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Barrett E. L., Jackson C. E., Fukumoto H. T., Chang G. W. Formate dehydrogenase mutants of Salmonella typhimurium: a new medium for their isolation and new mutant classes. Mol Gen Genet. 1979;177(1):95–101. doi: 10.1007/BF00267258. [DOI] [PubMed] [Google Scholar]
  21. Barrett E. L., Kwan H. S. Bacterial reduction of trimethylamine oxide. Annu Rev Microbiol. 1985;39:131–149. doi: 10.1146/annurev.mi.39.100185.001023. [DOI] [PubMed] [Google Scholar]
  22. Barrett E. L., Kwan H. S., Macy J. Anaerobiosis, formate, nitrate, and pyrA are involved in the regulation of formate hydrogenlyase in Salmonella typhimurium. J Bacteriol. 1984 Jun;158(3):972–977. doi: 10.1128/jb.158.3.972-977.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Barrett E. L., Riggs D. L. Evidence of a second nitrate reductase activity that is distinct from the respiratory enzyme in Salmonella typhimurium. J Bacteriol. 1982 May;150(2):563–571. doi: 10.1128/jb.150.2.563-571.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Barrett E. L., Riggs D. L. Salmonella typhimurium mutants defective in the formate dehydrogenase linked to nitrate reductase. J Bacteriol. 1982 Feb;149(2):554–560. doi: 10.1128/jb.149.2.554-560.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Bilous P. T., Weiner J. H. Dimethyl sulfoxide reductase activity by anaerobically grown Escherichia coli HB101. J Bacteriol. 1985 Jun;162(3):1151–1155. doi: 10.1128/jb.162.3.1151-1155.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Bilous P. T., Weiner J. H. Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grown Escherichia coli HB101. J Bacteriol. 1985 Jul;163(1):369–375. doi: 10.1128/jb.163.1.369-375.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Birkmann A., Sawers R. G., Böck A. Involvement of the ntrA gene product in the anaerobic metabolism of Escherichia coli. Mol Gen Genet. 1987 Dec;210(3):535–542. doi: 10.1007/BF00327209. [DOI] [PubMed] [Google Scholar]
  28. Birkmann A., Zinoni F., Sawers G., Böck A. Factors affecting transcriptional regulation of the formate-hydrogen-lyase pathway of Escherichia coli. Arch Microbiol. 1987 Jun;148(1):44–51. doi: 10.1007/BF00429646. [DOI] [PubMed] [Google Scholar]
  29. Bonnefoy-Orth V., Lepelletier M., Pascal M. C., Chippaux M. Nitrate reductase and cytochrome bnitrate reductase structural genes as parts of the nitrate reductase operon. Mol Gen Genet. 1981;181(4):535–540. doi: 10.1007/BF00428749. [DOI] [PubMed] [Google Scholar]
  30. Bonnefoy V., Burini J. F., Giordano G., Pascal M. C., Chippaux M. Presence in the 'silent' terminus region of the Escherichia coli K12 chromosome of cryptic gene(s) encoding a new nitrate reductase. Mol Microbiol. 1987 Sep;1(2):143–150. doi: 10.1111/j.1365-2958.1987.tb00506.x. [DOI] [PubMed] [Google Scholar]
  31. Bonnefoy V., Pascal M. C., Ratouchniak J., Chippaux M. Alteration by mutation of the control by oxygen of the nar operon in Escherichia coli. Mol Gen Genet. 1986 Nov;205(2):349–352. doi: 10.1007/BF00430449. [DOI] [PubMed] [Google Scholar]
  32. Bonnefoy V., Pascal M. C., Ratouchniak J., Chippaux M. Autoregulation of the nar operon encoding nitrate reductase in Escherichia coli. Mol Gen Genet. 1986 Jul;204(1):180–184. doi: 10.1007/BF00330207. [DOI] [PubMed] [Google Scholar]
  33. Boonstra J., Huttunen M. T., Konings W. N. Anaerobic transport in Escherichia coli membrane vesicles. J Biol Chem. 1975 Sep 10;250(17):6792–6798. [PubMed] [Google Scholar]
  34. Boonstra J., Konings W. N. Generation of an electrochemical proton gradient by nitrate respiration in membrane vesicles from anaerobically grown Escherichia coli. Eur J Biochem. 1977 Sep;78(2):361–368. doi: 10.1111/j.1432-1033.1977.tb11748.x. [DOI] [PubMed] [Google Scholar]
  35. Boonstra J., Sips H. J., Konings W. N. Active transport by membrane vesicles from anaerobically grown Escherichia coli energized by electron transfer to ferricyanide and chlorate. Eur J Biochem. 1976 Oct 1;69(1):35–44. doi: 10.1111/j.1432-1033.1976.tb10855.x. [DOI] [PubMed] [Google Scholar]
  36. Bosma H. J., Wever R., van 't Riet J. Electron paramagnetic resonance studies on membrane-bound respiratory nitrate reductase of Klebsiella aerogenes. FEBS Lett. 1978 Jun 1;90(1):107–111. doi: 10.1016/0014-5793(78)80308-1. [DOI] [PubMed] [Google Scholar]
  37. Boxer D. H., Clegg R. A. A transmembrane location for the proton-translocating reduced ubiquinone leads to nitrate reductase segment of the respiration chain of Escherichia coli. FEBS Lett. 1975 Dec 1;60(1):54–57. doi: 10.1016/0014-5793(75)80417-0. [DOI] [PubMed] [Google Scholar]
  38. Boxer D. H., Low D. C., Pommier J., Giordano G. Involvement of a low-molecular-weight substance in in vitro activation of the molybdoenzyme respiratory nitrate reductase from a chlB mutant of Escherichia coli. J Bacteriol. 1987 Oct;169(10):4678–4685. doi: 10.1128/jb.169.10.4678-4685.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Bray R. C., Vincent S. P., Lowe D. J., Clegg R. A., Garland P. B. Electron-paramagnetic-resonance studies on the molybdenum of nitrate reductase from Escherichia coli K12. Biochem J. 1976 Apr 1;155(1):201–203. doi: 10.1042/bj1550201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Brown T. D., Jones-Mortimer M. C., Kornberg H. L. The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J Gen Microbiol. 1977 Oct;102(2):327–336. doi: 10.1099/00221287-102-2-327. [DOI] [PubMed] [Google Scholar]
  41. Brown T. D., Pereira C. R., Stormer F. C. Studies of the acetate kinase-phosphotransacetylase and the butanediol-forming systems in Aerobacter aerogenes. J Bacteriol. 1972 Dec;112(3):1106–1111. doi: 10.1128/jb.112.3.1106-1111.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Buck M., Ames B. N. A modified nucleotide in tRNA as a possible regulator of aerobiosis: synthesis of cis-2-methyl-thioribosylzeatin in the tRNA of Salmonella. Cell. 1984 Feb;36(2):523–531. doi: 10.1016/0092-8674(84)90245-9. [DOI] [PubMed] [Google Scholar]
  43. Buxton R. S., Drury L. S. Identification of the dye gene product, mutational loss of which alters envelope protein composition and also affects sex factor F expression in Escherichia coli K-12. Mol Gen Genet. 1984;194(1-2):241–247. doi: 10.1007/BF00383523. [DOI] [PubMed] [Google Scholar]
  44. COHN M., HORIBATA K. Physiology of the inhibition by glucose of the induced synthesis of the beta-galactosideenzyme system of Escherichia coli. J Bacteriol. 1959 Nov;78:624–635. doi: 10.1128/jb.78.5.624-635.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Campbell A. M., del Campillo-Campbell A., Villaret D. B. Molybdate reduction by Escherichia coli K-12 and its chl mutants. Proc Natl Acad Sci U S A. 1985 Jan;82(1):227–231. doi: 10.1073/pnas.82.1.227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Carter K., Gennis R. B. Reconstitution of the Ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex. J Biol Chem. 1985 Sep 15;260(20):10986–10990. [PubMed] [Google Scholar]
  47. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  48. Casse F., Chippaux M., Pascal M. C. Isolation from Salmonella typhimurium LT2 of mutants lacking specifically nitrate reductase activity and mapping of the chl-C gene. Mol Gen Genet. 1973 Aug 17;124(3):247–251. doi: 10.1007/BF00293095. [DOI] [PubMed] [Google Scholar]
  49. Casse F. Mapping of the gene chl-B controlling membran bound nitrate reductase and formic hydrogen-lyase activities in Escherichia coli K 12. Biochem Biophys Res Commun. 1970 May 11;39(3):429–436. doi: 10.1016/0006-291x(70)90596-6. [DOI] [PubMed] [Google Scholar]
  50. Casse F., Pascal M. C., Chippaux M., Ratouchniak J. Mapping of the chl-B gene in Salmonella typhimurium LT2. Mol Gen Genet. 1972;119(1):67–70. doi: 10.1007/BF00270445. [DOI] [PubMed] [Google Scholar]
  51. Chaudhry G. R., Chaiken I. M., MacGregor C. H. An activity from Escherichia coli membranes responsible for the modification of nitrate reductase to its precursor form. J Biol Chem. 1983 May 10;258(9):5828–5833. [PubMed] [Google Scholar]
  52. Chaudhry G. R., MacGregor C. H. Cytochrome b from Escherichia coli nitrate reductase. Its properties and association with the enzyme complex. J Biol Chem. 1983 May 10;258(9):5819–5827. [PubMed] [Google Scholar]
  53. Chaudhry G. R., MacGregor C. H. Escherichia coli nitrate reductase subunit A: its role as the catalytic site and evidence for its modification. J Bacteriol. 1983 Apr;154(1):387–394. doi: 10.1128/jb.154.1.387-394.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Chippaux M., Bonnefoy-Orth V., Ratouchniak J., Pascal M. C. Operon fusions in the nitrate reductase operon and study of the control gene nir R in Escherichia coli. Mol Gen Genet. 1981;182(3):477–479. doi: 10.1007/BF00293938. [DOI] [PubMed] [Google Scholar]
  55. Chippaux M., Casse F., Pascal M. C. Isolation and phenotypes of mutants from Salmonella typhimurium defective in formate hydrogenlyase activity. J Bacteriol. 1972 May;110(2):766–768. doi: 10.1128/jb.110.2.766-768.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Chippaux M., Giudici D., Abou-Jaoudé A., Casse F., Pascal M. C. Laboratoire de Chimie Bactérienne C.N.R.S., Marsielle, France. Mol Gen Genet. 1978 Apr 6;160(2):225–229. doi: 10.1007/BF00267485. [DOI] [PubMed] [Google Scholar]
  57. Chippaux M., Pascal M. C., Casse F. Formate hydrogenlyase system in Salmonella typhimurium LT2. Eur J Biochem. 1977 Jan 3;72(1):149–155. doi: 10.1111/j.1432-1033.1977.tb11234.x. [DOI] [PubMed] [Google Scholar]
  58. Chippaux M., Pichinoty F. Les nitrate-réductases bactériennes. V. Induction de la biosynthèse de l'enzyme A par l'azoture. Arch Mikrobiol. 1970;71(4):361–366. [PubMed] [Google Scholar]
  59. Claassen V. P., Oltmann L. F., Bus S., v 't Riet J., Stouthamer A. H. The influence of growth conditions on the synthesis of molybdenum cofactor in Proteins mirabilis. Arch Microbiol. 1981 Sep;130(1):44–49. doi: 10.1007/BF00527070. [DOI] [PubMed] [Google Scholar]
  60. Clark D., Cronan J. E., Jr Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase. J Bacteriol. 1980 Jan;141(1):177–183. doi: 10.1128/jb.141.1.177-183.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Clegg R. A. Purification and some properties of nitrate reductase (EC 1.7.99.4) from Escherichia coli K12. Biochem J. 1976 Mar 1;153(3):533–541. doi: 10.1042/bj1530533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Cole J. A., Coleman K. J., Compton B. E., Kavanagh B. M., Keevil C. W. Nitrite and ammonia assimilation by anaerobic continuous cultures of Escherichia coli. J Gen Microbiol. 1974 Nov;85(1):11–22. doi: 10.1099/00221287-85-1-11. [DOI] [PubMed] [Google Scholar]
  63. Cole J. A. Cytochrome c552 and nitrite reduction in Escherichia coli. Biochim Biophys Acta. 1968 Oct 1;162(3):356–368. doi: 10.1016/0005-2728(68)90122-9. [DOI] [PubMed] [Google Scholar]
  64. Cole J. A., Newman B. M., White P. Biochemical and genetic characterization of nirB mutants of Escherichia coli K 12 pleiotropically defective in nitrite and sulphite reduction. J Gen Microbiol. 1980 Oct;120(2):475–483. doi: 10.1099/00221287-120-2-475. [DOI] [PubMed] [Google Scholar]
  65. Cole J. A., Ward F. B. Nitrite reductase-deficient mutants of Escherichia coli K12. J Gen Microbiol. 1973 May;76(1):21–29. doi: 10.1099/00221287-76-1-21. [DOI] [PubMed] [Google Scholar]
  66. Cole J. A., Wimpenny J. W. Metabolic pathways for nitrate reduction in Escherichia coli. Biochim Biophys Acta. 1968 Jul 16;162(1):39–48. doi: 10.1016/0005-2728(68)90212-0. [DOI] [PubMed] [Google Scholar]
  67. Cole S. T., Condon C., Lemire B. D., Weiner J. H. Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli. Biochim Biophys Acta. 1985 Dec;811(4):381–403. doi: 10.1016/0304-4173(85)90008-4. [DOI] [PubMed] [Google Scholar]
  68. Coleman K. J., Cornish-Bowden A., Cole J. A. Purification and properties of nitrite reductase from Escherichia coli K12. Biochem J. 1978 Nov 1;175(2):483–493. doi: 10.1042/bj1750483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Courtright J. B., Henning U. Malate dehydrogenase mutants in Escherichia coli K-12. J Bacteriol. 1970 Jun;102(3):722–728. doi: 10.1128/jb.102.3.722-728.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Cove D. J. Genetic studies of nitrate assimilation in Aspergillus nidulans. Biol Rev Camb Philos Soc. 1979 Aug;54(3):291–327. doi: 10.1111/j.1469-185x.1979.tb01014.x. [DOI] [PubMed] [Google Scholar]
  71. Cox J. C., Edwards E. S., DeMoss J. A. Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli. J Bacteriol. 1981 Mar;145(3):1317–1324. doi: 10.1128/jb.145.3.1317-1324.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Creaghan I. T., Guest J. R. Succinate dehydrogenase-dependent nutritional requirement for succinate in mutants of Escherichia coli K12. J Gen Microbiol. 1978 Jul;107(1):1–13. doi: 10.1099/00221287-107-1-1. [DOI] [PubMed] [Google Scholar]
  73. DOBROGOSZ W. J. THE INFLUENCE OF NITRATE AND NITRITE REDUCTION ON CATABOLITE REPRESSION IN ESCHERICHIA COLI. Biochim Biophys Acta. 1965 May 4;100:553–566. doi: 10.1016/0304-4165(65)90025-5. [DOI] [PubMed] [Google Scholar]
  74. De Groot G. N., Stouthamer A. H. Regulation of reductase formation in Proteus mirabilis. I. Formation of reductases and enzymes of the formic hydrogenlyase complex in the wild type and in chlorate-resistant mutants. Arch Mikrobiol. 1969;66(3):220–233. [PubMed] [Google Scholar]
  75. De Groot G. N., Stouthamer A. H. Regulation of reductase formation in Proteus mirabilis. II. Influence of growth with azide and of haem deficiency on nitrate reductase formation. Biochim Biophys Acta. 1970 Jun;208(3):414–427. doi: 10.1016/0304-4165(70)90214-x. [DOI] [PubMed] [Google Scholar]
  76. DeMoss J. A. Limited proteolysis of nitrate reductase purified from membranes of Escherichia coli. J Biol Chem. 1977 Mar 10;252(5):1696–1701. [PubMed] [Google Scholar]
  77. DeMoss J. A. Role of the chlC gene in formation of the formate-nitrate reductase pathway in Escherichia coli. J Bacteriol. 1978 Feb;133(2):626–630. doi: 10.1128/jb.133.2.626-630.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Dobrogosz W. J. Altered end-product patterns and catabolite repression in Escherichia coli. J Bacteriol. 1966 Jun;91(6):2263–2269. doi: 10.1128/jb.91.6.2263-2269.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Douglas M. W., Ward F. B., Cole J. A. The formate hydrogenlyase activity of cytochrome c552-deficient mutants of Escherichia coli K12. J Gen Microbiol. 1974 Feb;80(2):557–560. doi: 10.1099/00221287-80-2-557. [DOI] [PubMed] [Google Scholar]
  80. Dubourdieu M., Andrade E., Puig J. Molybdenum and chlorate resistant mutants in Escherichia coli K12. Biochem Biophys Res Commun. 1976 Jun 7;70(3):766–773. doi: 10.1016/0006-291x(76)90658-6. [DOI] [PubMed] [Google Scholar]
  81. Edwards E. S., Rondeau S. S., DeMoss J. A. chlC (nar) operon of Escherichia coli includes structural genes for alpha and beta subunits of nitrate reductase. J Bacteriol. 1983 Mar;153(3):1513–1520. doi: 10.1128/jb.153.3.1513-1520.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Ehrmann M., Boos W., Ormseth E., Schweizer H., Larson T. J. Divergent transcription of the sn-glycerol-3-phosphate active transport (glpT) and anaerobic sn-glycerol-3-phosphate dehydrogenase (glpA glpC glpB) genes of Escherichia coli K-12. J Bacteriol. 1987 Feb;169(2):526–532. doi: 10.1128/jb.169.2.526-532.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Enoch H. G., Lester R. L. Effects of molybdate, tungstate, and selenium compounds on formate dehydrogenase and other enzyme systems in Escherichia coli. J Bacteriol. 1972 Jun;110(3):1032–1040. doi: 10.1128/jb.110.3.1032-1040.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Enoch H. G., Lester R. L. The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. J Biol Chem. 1975 Sep 10;250(17):6693–6705. [PubMed] [Google Scholar]
  85. Enoch H. G., Lester R. L. The role of a novel cytochrome b-containing nitrate reductase and quinone in the in vitro reconstruction of formate-nitrate reductase activity of E. coli. Biochem Biophys Res Commun. 1974 Dec 23;61(4):1234–1241. doi: 10.1016/s0006-291x(74)80416-x. [DOI] [PubMed] [Google Scholar]
  86. FORGET P., PICHINOTY F. INFLUENCE DE LA RESPIRATION ANA'EROBIE DU NITRATE ET DU FUMARATE SUR LE M'ETABOLISME FERMENTAIRE D'AEROBACTER AEROGENES. Biochim Biophys Acta. 1964 Feb 10;82:441–444. doi: 10.1016/0304-4165(64)90328-9. [DOI] [PubMed] [Google Scholar]
  87. Fimmel A. L., Haddock B. A. Use of chlC-lac fusions to determine regulation of gene chlC in Escherichia coli K-12. J Bacteriol. 1979 Jun;138(3):726–730. doi: 10.1128/jb.138.3.726-730.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Forget P., Pichinoty F. Le cycle tricarboxyliue chez Aerobacter aerogenes. Ann Inst Pasteur (Paris) 1967 Mar;112(3):261–290. [PubMed] [Google Scholar]
  89. Forget P. The bacterial nitrate reductases. Solubilization, purification and properties of the enzyme A of Escherichia coli K 12. Eur J Biochem. 1974 Mar 1;42(2):325–332. doi: 10.1111/j.1432-1033.1974.tb03343.x. [DOI] [PubMed] [Google Scholar]
  90. Freedberg W. B., Lin E. C. Three kinds of controls affecting the expression of the glp regulon in Escherichia coli. J Bacteriol. 1973 Sep;115(3):816–823. doi: 10.1128/jb.115.3.816-823.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Fujita T., Sato Y. Studies on soluble cytochromes in Enterobacteriaceae. V. Nitrite-dependent gas evolution in cells containing cytochrome c-552. J Biochem. 1967 Aug;62(2):230–238. doi: 10.1093/oxfordjournals.jbchem.a128653. [DOI] [PubMed] [Google Scholar]
  92. GEST H. Oxidation and evolution of molecular hydrogen by microorganisms. Bacteriol Rev. 1954 Mar;18(1):43–73. doi: 10.1128/br.18.1.43-73.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. GEST H., PECK H. D., Jr A study of the hydrogenlyase reaction with systems derived from normal and anaerogenic coli-aerogenes bacteria. J Bacteriol. 1955 Sep;70(3):326–334. doi: 10.1128/jb.70.3.326-334.1955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. GORINI L., MAAS W. K. The potential for the formation of a biosynthetic enzyme in Escherichia coli. Biochim Biophys Acta. 1957 Jul;25(1):208–209. doi: 10.1016/0006-3002(57)90450-x. [DOI] [PubMed] [Google Scholar]
  95. GRAY C. T., GEST H. BIOLOGICAL FORMATION OF MOLECULAR HYDROGEN. Science. 1965 Apr 9;148(3667):186–192. doi: 10.1126/science.148.3667.186. [DOI] [PubMed] [Google Scholar]
  96. Garland P. B., Downie J. A., Haddock B. A. Proton translocation and the respiratory nitrate reductase of Escherichia coli. Biochem J. 1975 Dec;152(3):547–559. doi: 10.1042/bj1520547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. George G. N., Bray R. C., Morpeth F. F., Boxer D. H. Complexes with halide and other anions of the molybdenum centre of nitrate reductase from Escherichia coli. Biochem J. 1985 May 1;227(3):925–931. doi: 10.1042/bj2270925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Georgiou C. D., Fang H., Gennis R. B. Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli. J Bacteriol. 1987 May;169(5):2107–2112. doi: 10.1128/jb.169.5.2107-2112.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Giordano G., Graham A., Boxer D. H., Haddock B. A., Azoulay E. Characterization of the membrane-bound nitrate reductase activity of aerobically grown chlorate-sensitive mutants of Escherichia coli K12. FEBS Lett. 1978 Nov 15;95(2):290–294. doi: 10.1016/0014-5793(78)81013-8. [DOI] [PubMed] [Google Scholar]
  100. Giordano G., Grillet L., Pommier J., Terriere C., Haddock B. A., Azoulay E. Precursor forms of the subunits of nitrate reductase in chlA and chlB mutants of Escherichia coli K12. Eur J Biochem. 1980 Apr;105(2):297–306. doi: 10.1111/j.1432-1033.1980.tb04501.x. [DOI] [PubMed] [Google Scholar]
  101. Giordano G., Grillet L., Rosset R., Dou J. H., Azoulay E., Haddock B. A. Characterization of an Escherichia coli K12 mutant that is sensitive to chlorate when grown aerobically. Biochem J. 1978 Nov 15;176(2):553–561. doi: 10.1042/bj1760553. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Giordano G., Santini C. L., Saracino L., Iobbi C. Involvement of a protein with molybdenum cofactor in the in vitro activation of nitrate reductase from a chlA mutant of Escherichia coli K12. Biochim Biophys Acta. 1987 Aug 21;914(3):220–232. doi: 10.1016/0167-4838(87)90281-0. [DOI] [PubMed] [Google Scholar]
  103. Giordano G., Saracino L., Grillet L. Identification in various chlorate-resistant mutants of a protein involved in the activation of nitrate reductase in the soluble fraction of a chlA mutant of Escherichia coli K-12. Biochim Biophys Acta. 1985 Apr 17;839(2):181–190. doi: 10.1016/0304-4165(85)90035-2. [DOI] [PubMed] [Google Scholar]
  104. Giordano G., Violet M., Medani C. L., Pommier J. A common pathway for the activation of several molybdoenzymes in Escherichia coli K12. Biochim Biophys Acta. 1984 Apr 10;798(2):216–225. doi: 10.1016/0304-4165(84)90307-6. [DOI] [PubMed] [Google Scholar]
  105. Glaser J. H., DeMoss J. A. Comparison of nitrate reductase mutants of Escherichia coli selected by alternative procedures. Mol Gen Genet. 1972;116(1):1–10. doi: 10.1007/BF00334254. [DOI] [PubMed] [Google Scholar]
  106. Glaser J. H., DeMoss J. A. Phenotypic restoration by molybdate of nitrate reductase activity in chlD mutants of Escherichia coli. J Bacteriol. 1971 Nov;108(2):854–860. doi: 10.1128/jb.108.2.854-860.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Goldberg I., Nadler V., Hochman A. Mechanism of nitrogenase switch-off by oxygen. J Bacteriol. 1987 Feb;169(2):874–879. doi: 10.1128/jb.169.2.874-879.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Graham A., Boxer D. H. Arrangement of respiratory nitrate reductase in the cytoplasmic membrane of Escherichia coli. Location of beta subunit. FEBS Lett. 1980 Apr 21;113(1):15–20. doi: 10.1016/0014-5793(80)80484-4. [DOI] [PubMed] [Google Scholar]
  109. Graham A., Boxer D. H., Haddock B. A., Mandrand-Berthelot A. M., Jones R. W. Immunochemical analysis of the membrane-bound hydrogenase of Escherichia coli. FEBS Lett. 1980 May 5;113(2):167–172. doi: 10.1016/0014-5793(80)80584-9. [DOI] [PubMed] [Google Scholar]
  110. Graham A., Boxer D. H. The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli. Biochem J. 1981 Jun 1;195(3):627–637. doi: 10.1042/bj1950627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Grassi H. C., Andrade E., Puig J. Nitrate reductase and the membrane composition of pleiotropic chlorate resistant mutants of Escherichia coli K-12. Biochem Biophys Res Commun. 1979 Sep 12;90(1):86–91. doi: 10.1016/0006-291x(79)91593-6. [DOI] [PubMed] [Google Scholar]
  112. Gray C. T., Wimpenny J. W., Hughes D. E., Mossman M. R. Regulation of metabolism in facultative bacteria. I. Structural and functional changes in Escherichia coli associated with shifts between the aerobic and anaerobic states. Biochim Biophys Acta. 1966 Mar 28;117(1):22–32. doi: 10.1016/0304-4165(66)90148-6. [DOI] [PubMed] [Google Scholar]
  113. Gray C. T., Wimpenny J. W., Mossman M. R. Regulation of metabolism in facultative bacteria. II. Effects of aerobiosis, anaerobiosis and nutrition on the formation of Krebs cycle enzymes in Escherichia coli. Biochim Biophys Acta. 1966 Mar 28;117(1):33–41. doi: 10.1016/0304-4165(66)90149-8. [DOI] [PubMed] [Google Scholar]
  114. Green D. E., Haard N. F., Lenaz G., Silman H. I. On the noncatalytic proteins of membrane systems. Proc Natl Acad Sci U S A. 1968 May;60(1):277–284. doi: 10.1073/pnas.60.1.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Green D. E., Stickland L. H., Tarr H. L. Studies on reversible dehydrogenase systems: Carrier-linked reactions between isolated dehydrogenases. Biochem J. 1934;28(5):1812–1824. doi: 10.1042/bj0281812. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Green G. N., Gennis R. B. Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. J Bacteriol. 1983 Jun;154(3):1269–1275. doi: 10.1128/jb.154.3.1269-1275.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Green G. N., Kranz R. G., Lorence R. M., Gennis R. B. Identification of subunit I as the cytochrome b558 component of the cytochrome d terminal oxidase complex of Escherichia coli. J Biol Chem. 1984 Jun 25;259(12):7994–7997. [PubMed] [Google Scholar]
  118. Green G. N., Lorence R. M., Gennis R. B. Specific overproduction and purification of the cytochrome b558 component of the cytochrome d complex from Escherichia coli. Biochemistry. 1986 May 6;25(9):2309–2314. doi: 10.1021/bi00357a002. [DOI] [PubMed] [Google Scholar]
  119. Griffiths L., Cole J. A. Lack of redox control of the anaerobically-induced nirB+ gene of Escherichia coli K-12. Arch Microbiol. 1987 May;147(4):364–369. doi: 10.1007/BF00406134. [DOI] [PubMed] [Google Scholar]
  120. Grillet L., Giordano G. Identification and purification of a protein involved in the activation of nitrate reductase in the soluble fraction of a chlA mutant of Escherichia coli K12. Biochim Biophys Acta. 1983 Nov 28;749(1):115–124. doi: 10.1016/0167-4838(83)90158-9. [DOI] [PubMed] [Google Scholar]
  121. Guerrero M. G., Vega J. M., Leadbetter E., Losada M. Preparation and characterization of a soluble nitrate reductase from Azotobacter chroococcum. Arch Mikrobiol. 1973 Jun 25;91(4):287–304. doi: 10.1007/BF00425049. [DOI] [PubMed] [Google Scholar]
  122. Guest J. R. Biochemical and genetic studies with nitrate reductase C-gene mutants of Escherichia coli. Mol Gen Genet. 1969;105(4):285–297. doi: 10.1007/BF00277583. [DOI] [PubMed] [Google Scholar]
  123. Gutnick D., Calvo J. M., Klopotowski T., Ames B. N. Compounds which serve as the sole source of carbon or nitrogen for Salmonella typhimurium LT-2. J Bacteriol. 1969 Oct;100(1):215–219. doi: 10.1128/jb.100.1.215-219.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. HACKENTHAL E., MANNHEIM W., HACKENTHAL R., BECHER R. DIE REDUKTION VON PERCHLORAT DURCH BAKTERIEN. I. UNTERSUCHUNGEN AN INTAKTEN ZELLEN. Biochem Pharmacol. 1964 Feb;13:195–206. doi: 10.1016/0006-2952(64)90137-6. [DOI] [PubMed] [Google Scholar]
  125. HADJIPETROU L. P., STOUTHAMER A. H. ENERGY PRODUCTION DURING NITRATE RESPIRATION BY AEROBACTER AEROGENES. J Gen Microbiol. 1965 Jan;38:29–34. doi: 10.1099/00221287-38-1-29. [DOI] [PubMed] [Google Scholar]
  126. Hackett C. S., MacGregor C. H. Synthesis and degradation of nitrate reductase in Escherichia coli. J Bacteriol. 1981 Apr;146(1):352–359. doi: 10.1128/jb.146.1.352-359.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Hackett N. R., Bragg P. D. Membrane cytochromes of Escherichia coli chl mutants. J Bacteriol. 1983 May;154(2):719–727. doi: 10.1128/jb.154.2.719-727.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Hackett N. R., Bragg P. D. Membrane cytochromes of Escherichia coli grown aerobically and anaerobically with nitrate. J Bacteriol. 1983 May;154(2):708–718. doi: 10.1128/jb.154.2.708-718.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Haddock B. A., Jones C. W. Bacterial respiration. Bacteriol Rev. 1977 Mar;41(1):47–99. doi: 10.1128/br.41.1.47-99.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. Haddock B. A., Kendall-Tobias M. W. Functional anaerobic electron transport linked to the reduction of nitrate and fumarate in membranes from Escherichia coli as demonstrated by quenching of atebrin fluorescence. Biochem J. 1975 Dec;152(3):655–659. doi: 10.1042/bj1520655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  131. Hahn S., Schleif R. In vivo regulation of the Escherichia coli araC promoter. J Bacteriol. 1983 Aug;155(2):593–600. doi: 10.1128/jb.155.2.593-600.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  132. Hamamoto T., Carrasco N., Matsushita K., Kaback H. R., Montal M. Direct measurement of the electrogenic activity of o-type cytochrome oxidase from Escherichia coli reconstituted into planar lipid bilayers. Proc Natl Acad Sci U S A. 1985 May;82(9):2570–2573. doi: 10.1073/pnas.82.9.2570. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Harley C. B., Reynolds R. P. Analysis of E. coli promoter sequences. Nucleic Acids Res. 1987 Mar 11;15(5):2343–2361. doi: 10.1093/nar/15.5.2343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  134. Harman J. G., McKenney K., Peterkofsky A. Structure-function analysis of three cAMP-independent forms of the cAMP receptor protein. J Biol Chem. 1986 Dec 15;261(35):16332–16339. [PubMed] [Google Scholar]
  135. Hawkes T. R., Bray R. C. Quantitative transfer of the molybdenum cofactor from xanthine oxidase and from sulphite oxidase to the deficient enzyme of the nit-1 mutant of Neurospora crassa to yield active nitrate reductase. Biochem J. 1984 Apr 15;219(2):481–493. doi: 10.1042/bj2190481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Hertz R., Bar-Tana J. Reductive repression in Escherichia coli K-12 is mediated by oxygen radicals. Arch Biochem Biophys. 1986 Oct;250(1):54–62. doi: 10.1016/0003-9861(86)90701-0. [DOI] [PubMed] [Google Scholar]
  137. Hom S. S., Hennecke H., Shanmugam K. T. Regulation of nitrogenase biosynthesis in Klebsiella pneumoniae: effect of nitrate. J Gen Microbiol. 1980 Mar;117(1):169–179. doi: 10.1099/00221287-117-1-169. [DOI] [PubMed] [Google Scholar]
  138. ITAGAKI E. THE ROLE OF LIPOPHILIC QUINONES IN THE ELECTRON TRANSPORT SYSTEM OF ESCHERICHIA COLI. J Biochem. 1964 Apr;55:432–445. doi: 10.1093/oxfordjournals.jbchem.a127905. [DOI] [PubMed] [Google Scholar]
  139. Imperial J., Ugalde R. A., Shah V. K., Brill W. J. Mol- mutants of Klebsiella pneumoniae requiring high levels of molybdate for nitrogenase activity. J Bacteriol. 1985 Sep;163(3):1285–1287. doi: 10.1128/jb.163.3.1285-1287.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Ingledew W. J., Poole R. K. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–271. doi: 10.1128/mr.48.3.222-271.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. Iobbi C., Santini C. L., Bonnefoy V., Giordano G. Biochemical and immunological evidence for a second nitrate reductase in Escherichia coli K12. Eur J Biochem. 1987 Oct 15;168(2):451–459. doi: 10.1111/j.1432-1033.1987.tb13438.x. [DOI] [PubMed] [Google Scholar]
  142. Ishimoto M., Yamamoto I. Cell growth and metabolic products of Escherichia coli in nitrate respiration. Z Allg Mikrobiol. 1977;17(4):309–320. doi: 10.1002/jobm.3630170408. [DOI] [PubMed] [Google Scholar]
  143. Iuchi S., Kuritzkes D. R., Lin E. C. Escherichia coli mutant with altered respiratory control of the frd operon. J Bacteriol. 1985 Mar;161(3):1023–1028. doi: 10.1128/jb.161.3.1023-1028.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Iuchi S., Kuritzkes D. R., Lin E. C. Three classes of Escherichia coli mutants selected for aerobic expression of fumarate reductase. J Bacteriol. 1986 Dec;168(3):1415–1421. doi: 10.1128/jb.168.3.1415-1421.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  145. Iuchi S., Lin E. C. Molybdenum effector of fumarate reductase repression and nitrate reductase induction in Escherichia coli. J Bacteriol. 1987 Aug;169(8):3720–3725. doi: 10.1128/jb.169.8.3720-3725.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Iuchi S., Lin E. C. The narL gene product activates the nitrate reductase operon and represses the fumarate reductase and trimethylamine N-oxide reductase operons in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3901–3905. doi: 10.1073/pnas.84.11.3901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Jackson R. H., Cole J. A., Cornish-Bowden A. The steady state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12. The reduction of single-electron acceptors. Biochem J. 1982 May 1;203(2):505–510. doi: 10.1042/bj2030505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Jackson R. H., Cornish-Bowden A., Cole J. A. Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem J. 1981 Mar 1;193(3):861–867. doi: 10.1042/bj1930861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Jamieson D. J., Higgins C. F. Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium. J Bacteriol. 1984 Oct;160(1):131–136. doi: 10.1128/jb.160.1.131-136.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  150. Jamieson D. J., Higgins C. F. Two genetically distinct pathways for transcriptional regulation of anaerobic gene expression in Salmonella typhimurium. J Bacteriol. 1986 Oct;168(1):389–397. doi: 10.1128/jb.168.1.389-397.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Jamieson D. J., Sawers R. G., Rugman P. A., Boxer D. H., Higgins C. F. Effects of anaerobic regulatory mutations and catabolite repression on regulation of hydrogen metabolism and hydrogenase isoenzyme composition in Salmonella typhimurium. J Bacteriol. 1986 Oct;168(1):405–411. doi: 10.1128/jb.168.1.405-411.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  152. Jayaraman P. S., Peakman T. C., Busby S. J., Quincey R. V., Cole J. A. Location and sequence of the promoter of the gene for the NADH-dependent nitrite reductase of Escherichia coli and its regulation by oxygen, the Fnr protein and nitrite. J Mol Biol. 1987 Aug 20;196(4):781–788. doi: 10.1016/0022-2836(87)90404-9. [DOI] [PubMed] [Google Scholar]
  153. Jeter R. M., Sias S. R., Ingraham J. L. Chromosomal location and function of genes affecting Pseudomonas aeruginosa nitrate assimilation. J Bacteriol. 1984 Feb;157(2):673–677. doi: 10.1128/jb.157.2.673-677.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Johann S., Hinton S. M. Cloning and nucleotide sequence of the chlD locus. J Bacteriol. 1987 May;169(5):1911–1916. doi: 10.1128/jb.169.5.1911-1916.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. John P. Aerobic and anaerobic bacterial respiration monitored by electrodes. J Gen Microbiol. 1977 Jan;98(1):231–238. doi: 10.1099/00221287-98-1-231. [DOI] [PubMed] [Google Scholar]
  156. Johnson J. L., Hainline B. E., Rajagopalan K. V., Arison B. H. The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J Biol Chem. 1984 May 10;259(9):5414–5422. [PubMed] [Google Scholar]
  157. Johnson J. L., Hainline B. E., Rajagopalan K. V. Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component. J Biol Chem. 1980 Mar 10;255(5):1783–1786. [PubMed] [Google Scholar]
  158. Johnson M. E., Rajagopalan K. V. In vitro system for molybdopterin biosynthesis. J Bacteriol. 1987 Jan;169(1):110–116. doi: 10.1128/jb.169.1.110-116.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Johnson M. E., Rajagopalan K. V. Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis. J Bacteriol. 1987 Jan;169(1):117–125. doi: 10.1128/jb.169.1.117-125.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. Johnson M. K., Bennett D. E., Morningstar J. E., Adams M. W., Mortenson L. E. The iron-sulfur cluster composition of Escherichia coli nitrate reductase. J Biol Chem. 1985 May 10;260(9):5456–5463. [PubMed] [Google Scholar]
  161. Jones H. M., Gunsalus R. P. Regulation of Escherichia coli fumarate reductase (frdABCD) operon expression by respiratory electron acceptors and the fnr gene product. J Bacteriol. 1987 Jul;169(7):3340–3349. doi: 10.1128/jb.169.7.3340-3349.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  162. Jones H. M., Gunsalus R. P. Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate. J Bacteriol. 1985 Dec;164(3):1100–1109. doi: 10.1128/jb.164.3.1100-1109.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. Jones R. W., Garland P. B. Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane. Biochem J. 1977 Apr 15;164(1):199–211. doi: 10.1042/bj1640199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. Jones R. W., Lamont A., Garland P. B. The mechanism of proton translocation driven by the respiratory nitrate reductase complex of Escherichia coli. Biochem J. 1980 Jul 15;190(1):79–94. doi: 10.1042/bj1900079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Jones R. W. The role of the membrane-bound hydrogenase in the energy-conserving oxidation of molecular hydrogen by Escherichia coli. Biochem J. 1980 May 15;188(2):345–350. doi: 10.1042/bj1880345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  166. Jänel G., Michelsen U., Nishimura S., Kersten H. Queuosine modification in tRNA and expression of the nitrate reductase in Escherichia coli. EMBO J. 1984 Jul;3(7):1603–1608. doi: 10.1002/j.1460-2075.1984.tb02017.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  167. Kajie S., Anraku Y. Purification of a hexaheme cytochrome c552 from Escherichia coli K 12 and its properties as a nitrite reductase. Eur J Biochem. 1986 Jan 15;154(2):457–463. doi: 10.1111/j.1432-1033.1986.tb09419.x. [DOI] [PubMed] [Google Scholar]
  168. Kaprálek F., Jechová E., Otavová M. Two sites of oxygen control in induced synthesis of respiratory nitrate reductase in Escherichia coli. J Bacteriol. 1982 Mar;149(3):1142–1145. doi: 10.1128/jb.149.3.1142-1145.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  169. Kaprálek F. The physiological role of tetrathionate respiration in growing citrobacter. J Gen Microbiol. 1972 Jun;71(1):133–139. doi: 10.1099/00221287-71-1-133. [DOI] [PubMed] [Google Scholar]
  170. Kashket E. R. The proton motive force in bacteria: a critical assessment of methods. Annu Rev Microbiol. 1985;39:219–242. doi: 10.1146/annurev.mi.39.100185.001251. [DOI] [PubMed] [Google Scholar]
  171. Keevil C. W., Hough J. S., Cole J. A. Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate. J Gen Microbiol. 1979 Oct;114(2):355–359. doi: 10.1099/00221287-114-2-355. [DOI] [PubMed] [Google Scholar]
  172. Kemp J. D., Atkinson D. E. Nitrite reductase of Escherichia coli specific for reduced nicotinamide adenine dinucleotide. J Bacteriol. 1966 Sep;92(3):628–634. doi: 10.1128/jb.92.3.628-634.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Kita K., Kasahara M., Anraku Y. Formation of a membrane potential by reconstructed liposomes made with cytochrome b562-o complex, a terminal oxidase of Escherichia coli K12. J Biol Chem. 1982 Jul 25;257(14):7933–7935. [PubMed] [Google Scholar]
  174. Kita K., Konishi K., Anraku Y. Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth. J Biol Chem. 1984 Mar 10;259(5):3368–3374. [PubMed] [Google Scholar]
  175. Kita K., Konishi K., Anraku Y. Terminal oxidases of Escherichia coli aerobic respiratory chain. II. Purification and properties of cytochrome b558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems. J Biol Chem. 1984 Mar 10;259(5):3375–3381. [PubMed] [Google Scholar]
  176. Knook D. L., Planta R. J. Function of ubiquinone in electron transport from reduced nicotinamide adenine dinucleotide to nitrate and oxygen in Aerobacter aerogenes. J Bacteriol. 1971 Feb;105(2):483–488. doi: 10.1128/jb.105.2.483-488.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  177. Knowles R. Denitrification. Microbiol Rev. 1982 Mar;46(1):43–70. doi: 10.1128/mr.46.1.43-70.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  178. Kobayashi M., Ishimoto M. Aerobic inhibition of nitrate assimilation in Escherichia coli. Z Allg Mikrobiol. 1973;13(5):405–413. doi: 10.1002/jobm.3630130505. [DOI] [PubMed] [Google Scholar]
  179. Koland J. G., Miller M. J., Gennis R. B. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry. 1984 Jan 31;23(3):445–453. doi: 10.1021/bi00298a008. [DOI] [PubMed] [Google Scholar]
  180. Konings W. N., Kaback H. R. Anaerobic transport in Escherichia coli membrane vesicles. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3376–3381. doi: 10.1073/pnas.70.12.3376. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Kramer S., Hageman R. V., Rajagopalan K. V. In vitro reconstitution of nitrate reductase activity of the Neurospora crassa mutant nit-1: specific incorporation of molybdopterin. Arch Biochem Biophys. 1984 Sep;233(2):821–829. doi: 10.1016/0003-9861(84)90511-3. [DOI] [PubMed] [Google Scholar]
  182. Kranz R. G., Barassi C. A., Gennis R. B. Immunological analysis of the heme proteins present in aerobically grown Escherichia coli. J Bacteriol. 1984 Jun;158(3):1191–1194. doi: 10.1128/jb.158.3.1191-1194.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  183. Kranz R. G., Barassi C. A., Miller M. J., Green G. N., Gennis R. B. Immunological characterization of an Escherichia coli strain which is lacking cytochrome d. J Bacteriol. 1983 Oct;156(1):115–121. doi: 10.1128/jb.156.1.115-121.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  184. Kranz R. G., Gennis R. B. Characterization of the cytochrome d terminal oxidase complex of Escherichia coli using polyclonal and monoclonal antibodies. J Biol Chem. 1984 Jun 25;259(12):7998–8003. [PubMed] [Google Scholar]
  185. Kranz R. G., Gennis R. B. Immunological characterization of the cytochrome o terminal oxidase from Escherichia coli. J Biol Chem. 1983 Sep 10;258(17):10614–10621. [PubMed] [Google Scholar]
  186. Kristjansson J. K., Hollocher T. C. Substrate binding site for nitrate reductase of Escherichia coli is on the inner aspect of the membrane. J Bacteriol. 1979 Mar;137(3):1227–1233. doi: 10.1128/jb.137.3.1227-1233.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Kröger A., Dadák V., Klingenberg M., Diemer F. On the role of quinones in bacterial electron transport. Differential roles of ubiquinone and menaquinone in Proteus rettgeri. Eur J Biochem. 1971 Aug 16;21(3):322–333. doi: 10.1111/j.1432-1033.1971.tb01472.x. [DOI] [PubMed] [Google Scholar]
  188. Kröger A., Klingenberg M. Quinones and nicotinamide nucleotides associated with electron transfer. Vitam Horm. 1970;28:533–574. doi: 10.1016/s0083-6729(08)60910-3. [DOI] [PubMed] [Google Scholar]
  189. Kuritzkes D. R., Zhang X. Y., Lin E. C. Use of phi(glp-lac) in studies of respiratory regulation of the Escherichia coli anaerobic sn-glycerol-3-phosphate dehydrogenase genes (glpAB). J Bacteriol. 1984 Feb;157(2):591–598. doi: 10.1128/jb.157.2.591-598.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  190. Kwan H. S., Wong K. K. A general method for isolation of Mu d1-8(Aprlac) operon fusions in Salmonella typhimurium LT2 from Tn10 insertion strains: chlC::Mu d1-8. Mol Gen Genet. 1986 Nov;205(2):221–224. doi: 10.1007/BF00430431. [DOI] [PubMed] [Google Scholar]
  191. LINNANE A. W., WRIGLEY C. W. FRAGMENTATION OF THE ELECTRON TRANSPORT CHAIN OF ESCHERICHIA COLI. PREPARATION OF A SOLUBLE FORMATE DEHYDROGENASE-CYTOCHROME B1 COMPLEX. Biochim Biophys Acta. 1963 Nov 8;77:408–418. doi: 10.1016/0006-3002(63)90515-8. [DOI] [PubMed] [Google Scholar]
  192. Lambden P. R., Guest J. R. Mutants of Escherichia coli K12 unable to use fumarate as an anaerobic electron acceptor. J Gen Microbiol. 1976 Dec;97(2):145–160. doi: 10.1099/00221287-97-2-145. [DOI] [PubMed] [Google Scholar]
  193. Laszlo D. J., Fandrich B. L., Sivaram A., Chance B., Taylor B. L. Cytochrome o as a terminal oxidase and receptor for aerotaxis in Salmonella typhimurium. J Bacteriol. 1984 Aug;159(2):663–667. doi: 10.1128/jb.159.2.663-667.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  194. Lawford H. G., Haddock B. A. Respiration-driven proton translocation in Escherichia coli. Biochem J. 1973 Sep;136(1):217–220. doi: 10.1042/bj1360217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  195. Lee J. H., Dobrogosz W. J. Effects of aerobic and anaerobic shock on catabolite repression in cyclic AMP suppressor mutants of Escherichia coli. J Bacteriol. 1983 May;154(2):992–994. doi: 10.1128/jb.154.2.992-994.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  196. Lee J. H., Patel P., Sankar P., Shanmugam K. T. Isolation and characterization of mutant strains of Escherichia coli altered in H2 metabolism. J Bacteriol. 1985 Apr;162(1):344–352. doi: 10.1128/jb.162.1.344-352.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  197. Leinfelder W., Forchhammer K., Zinoni F., Sawers G., Mandrand-Berthelot M. A., Böck A. Escherichia coli genes whose products are involved in selenium metabolism. J Bacteriol. 1988 Feb;170(2):540–546. doi: 10.1128/jb.170.2.540-546.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  198. Lester R. L., DeMoss J. A. Effects of molybdate and selenite on formate and nitrate metabolism in Escherichia coli. J Bacteriol. 1971 Mar;105(3):1006–1014. doi: 10.1128/jb.105.3.1006-1014.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  199. Li S. F., DeMoss J. A. Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals. J Bacteriol. 1987 Oct;169(10):4614–4620. doi: 10.1128/jb.169.10.4614-4620.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Li S., Rabi T., DeMoss J. A. Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli. J Bacteriol. 1985 Oct;164(1):25–32. doi: 10.1128/jb.164.1.25-32.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  201. Lin E. C. Glycerol dissimilation and its regulation in bacteria. Annu Rev Microbiol. 1976;30:535–578. doi: 10.1146/annurev.mi.30.100176.002535. [DOI] [PubMed] [Google Scholar]
  202. Lorence R. M., Green G. N., Gennis R. B. Potentiometric analysis of the cytochromes of an Escherichia coli mutant strain lacking the cytochrome d terminal oxidase complex. J Bacteriol. 1984 Jan;157(1):115–121. doi: 10.1128/jb.157.1.115-121.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  203. Lorowitz W., Clark D. Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase. J Bacteriol. 1982 Nov;152(2):935–938. doi: 10.1128/jb.152.2.935-938.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  204. Lund K., DeMoss J. A. Association-dissociation behavior and subunit structure of heat-released nitrate reductase from Escherichia coli. J Biol Chem. 1976 Apr 25;251(8):2207–2216. [PubMed] [Google Scholar]
  205. MacDonald H., Pope N. R., Cole J. A. Isolation, characterization and complementation analysis of nirB mutants of Escherichia coli deficient only in NADH-dependent nitrite reductase activity. J Gen Microbiol. 1985 Oct;131(10):2771–2782. doi: 10.1099/00221287-131-10-2771. [DOI] [PubMed] [Google Scholar]
  206. MacGregor C. H. Anaerobic cytochrome b1 in Escherichia coli: association with and regulation of nitrate reductase. J Bacteriol. 1975 Mar;121(3):1111–1116. doi: 10.1128/jb.121.3.1111-1116.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  207. MacGregor C. H. Biosynthesis of membrane-bound nitrate reductase in Escherichia coli: evidence for a soluble precursor. J Bacteriol. 1976 Apr;126(1):122–131. doi: 10.1128/jb.126.1.122-131.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. MacGregor C. H., Bishop C. W., Blech J. E. Localization of proteolytic activity in the outer membrane of Escherichia coli. J Bacteriol. 1979 Jan;137(1):574–583. doi: 10.1128/jb.137.1.574-583.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. MacGregor C. H., Bishop C. W. Do cytochromes function as oxygen sensors in the regulation of nitrate reductase biosynthesis? J Bacteriol. 1977 Jul;131(1):372–373. doi: 10.1128/jb.131.1.372-373.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  210. MacGregor C. H., Christopher A. R. Asymmetric distribution of nitrate reductase subunits in the cytoplasmic membrane of Escherichia coli: evidence derived from surface labeling studies with transglutaminase. Arch Biochem Biophys. 1978 Jan 15;185(1):204–213. doi: 10.1016/0003-9861(78)90160-1. [DOI] [PubMed] [Google Scholar]
  211. MacGregor C. H., McElhaney G. E. New mechanism for post-translational processing during assembly of a cytoplasmic membrane protein? J Bacteriol. 1981 Nov;148(2):551–558. doi: 10.1128/jb.148.2.551-558.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  212. MacGregor C. H., Schnaitman C. A. Alterations in the cytoplasmic membrane proteins of various chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1971 Oct;108(1):564–570. doi: 10.1128/jb.108.1.564-570.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  213. MacGregor C. H., Schnaitman C. A. Nitrate reductase in E. coli: properties of the enzyme and in vitro reconstitution from enzyme-deficient mutants. J Supramol Struct. 1974;2(5-6):715–727. doi: 10.1002/jss.400020515. [DOI] [PubMed] [Google Scholar]
  214. MacGregor C. H., Schnaitman C. A., Normansell D. E. Purification and properties of nitrate reductase from Escherichia coli K12. J Biol Chem. 1974 Aug 25;249(16):5321–5327. [PubMed] [Google Scholar]
  215. MacGregor C. H., Schnaitman C. A. Reconstitution of nitrate reductase activity and formation of membrane particles from cytoplasmic extracts of chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1973 Jun;114(3):1164–1176. doi: 10.1128/jb.114.3.1164-1176.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  216. MacGregor C. H., Schnaitman C. A. Restoration of reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase activity of a Neurospora mutant by extracts of various chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1972 Oct;112(1):388–391. doi: 10.1128/jb.112.1.388-391.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  217. MacGregor C. H. Solubilization of Escherichia coli nitrate reductase by a membrane-bound protease. J Bacteriol. 1975 Mar;121(3):1102–1110. doi: 10.1128/jb.121.3.1102-1110.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  218. MacGregor C. H. Synthesis of nitrate reductase components in chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1975 Mar;121(3):1117–1121. doi: 10.1128/jb.121.3.1117-1121.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  219. Macdonald H., Cole J. Molecular cloning and functional analysis of the cysG and nirB genes of Escherichia coli K12, two closely-linked genes required for NADH-dependent nitrite reductase activity. Mol Gen Genet. 1985;200(2):328–334. doi: 10.1007/BF00425444. [DOI] [PubMed] [Google Scholar]
  220. Matsushita K., Kaback H. R. D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry. 1986 May 6;25(9):2321–2327. doi: 10.1021/bi00357a004. [DOI] [PubMed] [Google Scholar]
  221. Matsushita K., Patel L., Gennis R. B., Kaback H. R. Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli. Proc Natl Acad Sci U S A. 1983 Aug;80(16):4889–4893. doi: 10.1073/pnas.80.16.4889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  222. Matsushita K., Patel L., Kaback H. R. Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation. Biochemistry. 1984 Sep 25;23(20):4703–4714. doi: 10.1021/bi00315a028. [DOI] [PubMed] [Google Scholar]
  223. McKay D. B., Weber I. T., Steitz T. A. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP. J Biol Chem. 1982 Aug 25;257(16):9518–9524. [PubMed] [Google Scholar]
  224. McPherson M. J., Baron A. J., Pappin D. J., Wootton J. C. Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene. FEBS Lett. 1984 Nov 19;177(2):260–264. doi: 10.1016/0014-5793(84)81295-8. [DOI] [PubMed] [Google Scholar]
  225. Meganathan R., Schrementi J. Tetrahydrothiophene 1-oxide as an electron acceptor for Escherichia coli. J Bacteriol. 1987 Jun;169(6):2862–2865. doi: 10.1128/jb.169.6.2862-2865.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  226. Miki K., Lin E. C. Electron transport chain from glycerol 3-phosphate to nitrate in Escherichia coli. J Bacteriol. 1975 Dec;124(3):1288–1294. doi: 10.1128/jb.124.3.1288-1294.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  227. Miles J. S., Guest J. R. Molecular genetic aspects of the citric acid cycle of Escherichia coli. Biochem Soc Symp. 1987;54:45–65. [PubMed] [Google Scholar]
  228. Miller J. B., Amy N. K. Molybdenum cofactor in chlorate-resistant and nitrate reductase-deficient insertion mutants of Escherichia coli. J Bacteriol. 1983 Aug;155(2):793–801. doi: 10.1128/jb.155.2.793-801.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  229. Miller J. B., Scott D. J., Amy N. K. Molybdenum-sensitive transcriptional regulation of the chlD locus of Escherichia coli. J Bacteriol. 1987 May;169(5):1853–1860. doi: 10.1128/jb.169.5.1853-1860.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  230. Miller M. J., Gennis R. B. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J Biol Chem. 1985 Nov 15;260(26):14003–14008. [PubMed] [Google Scholar]
  231. Miller M. J., Gennis R. B. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem. 1983 Aug 10;258(15):9159–9165. [PubMed] [Google Scholar]
  232. Morpeth F. F., Boxer D. H. Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12. Biochemistry. 1985 Jan 1;24(1):40–46. doi: 10.1021/bi00322a007. [DOI] [PubMed] [Google Scholar]
  233. Murakami H., Kita K., Anraku Y. Purification and properties of a diheme cytochrome b561 of the Escherichia coli respiratory chain. J Biol Chem. 1986 Jan 15;261(2):548–551. [PubMed] [Google Scholar]
  234. NASON A. Symposium on metabolism of inorganic compounds. II. Enzymatic pathways of nitrate, nitrite, and hydroxylamine metabolisms. Bacteriol Rev. 1962 Mar;26:16–41. doi: 10.1128/br.26.1.16-41.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  235. NICHOLAS D. J., NASON A. Diphosphopyridine nucleotide-nitrate reductase from Escherichia coli. J Bacteriol. 1955 May;69(5):580–583. doi: 10.1128/jb.69.5.580-583.1955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  236. Nagatani H., Shimizu M., Valentine R. C. The mechanism of ammonia assimilation in nitrogen fixing Bacteria. Arch Mikrobiol. 1971;79(2):164–175. doi: 10.1007/BF00424923. [DOI] [PubMed] [Google Scholar]
  237. Nason A., Lee K. Y., Pan S. S., Ketchum P. A., Lamberti A., DeVries J. Invitro formation of assimilatory reduced nicotinamide adenine dinucleotide phosphate: nitrate reductase from a Neurospora mutant and a component of molybdenum-enzymes. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3242–3246. doi: 10.1073/pnas.68.12.3242. [DOI] [PMC free article] [PubMed] [Google Scholar]
  238. Newman B. M., Cole J. A. Lack of a regulatory function for glutamine synthetase protein in the synthesis of glutamate dehydrogenase and nitrite reductase in Escherichia coli K12. J Gen Microbiol. 1977 Feb;98(2):369–377. doi: 10.1099/00221287-98-2-369. [DOI] [PubMed] [Google Scholar]
  239. Newman B. M., Cole J. A. The chromosomal location and pleiotropic effects of mutations of the nirA+ gene of Escherichia coli K12: the essential role of nirA+ in nitrite reduction and in other anaerobic redox reactions. J Gen Microbiol. 1978 May;106(1):1–12. doi: 10.1099/00221287-106-1-1. [DOI] [PubMed] [Google Scholar]
  240. Nichol C. A., Smith G. K., Duch D. S. Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin. Annu Rev Biochem. 1985;54:729–764. doi: 10.1146/annurev.bi.54.070185.003501. [DOI] [PubMed] [Google Scholar]
  241. Noji S., Taniguchi S. Molecular oxygen controls nitrate transport of Escherichia coli nitrate-respiring cells. J Biol Chem. 1987 Jul 15;262(20):9441–9443. [PubMed] [Google Scholar]
  242. Okinaka R. T., Dobrogosz W. J. Catabolite repression and pyruvate metabolism in Escherichia coli. J Bacteriol. 1967 May;93(5):1644–1650. doi: 10.1128/jb.93.5.1644-1650.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  243. Oltmann L. F., Claassen V. P., Kastelein P., Reijnders W. N., Stouthamer A. H. Influence of tungstate on the formation and activities of four reductases in Proteus mirabilis: identification of two new molybdo-enzymes: chlorate reductase and tetrathionate reductase. FEBS Lett. 1979 Oct 1;106(1):43–46. doi: 10.1016/0014-5793(79)80691-2. [DOI] [PubMed] [Google Scholar]
  244. Oltmann L. F., Reijnders W. N., Stoughamer A. H. Characterization of purified nitrate reductase A and chlorate reductase C from Proteus mirabilis. Arch Microbiol. 1976 Dec 1;111(1-2):25–35. doi: 10.1007/BF00446546. [DOI] [PubMed] [Google Scholar]
  245. Orth V., Chippaux M., Pascal M. C. A mutant defective in electron transfer to nitrate in Escherichia coli K12. J Gen Microbiol. 1980 Mar;117(1):257–262. doi: 10.1099/00221287-117-1-257. [DOI] [PubMed] [Google Scholar]
  246. PECK H. D., Jr, GEST H. Formic dehydrogenase and the hydrogenlyase enzyme complex in coli-aerogenes bacteria. J Bacteriol. 1957 Jun;73(6):706–721. doi: 10.1128/jb.73.6.706-721.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  247. PICHINOTY F., D'ORNANO L. Inhibition by oxygen of biosynthesis and activity of nitrate-reductase in Aerobacter aerogenes. Nature. 1961 Aug 26;191:879–881. doi: 10.1038/191879a0. [DOI] [PubMed] [Google Scholar]
  248. PINSENT J. The need for selenite and molybdate in the formation of formic dehydrogenase by members of the coli-aerogenes group of bacteria. Biochem J. 1954 May;57(1):10–16. doi: 10.1042/bj0570010. [DOI] [PMC free article] [PubMed] [Google Scholar]
  249. Pascal M. C., Burini J. F., Chippaux M. Regulation of the trimethylamine N-oxide (TMAO) reductase in Escherichia coli: analysis of tor::Mud1 operon fusion. Mol Gen Genet. 1984;195(1-2):351–355. doi: 10.1007/BF00332770. [DOI] [PubMed] [Google Scholar]
  250. Pascal M. C., Burini J. F., Ratouchniak J., Chippaux M. Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes. Mol Gen Genet. 1982;188(1):103–106. doi: 10.1007/BF00333001. [DOI] [PubMed] [Google Scholar]
  251. Pascal M. C., Casse F., Chippaux M., Lepelletier M. Genetic analysis of mutants of Escherichia coli K12 and Salmonella typhimurium LT2 deficient in hydrogenase activity. Mol Gen Genet. 1975 Nov 24;141(2):173–179. doi: 10.1007/BF00267682. [DOI] [PubMed] [Google Scholar]
  252. Pascal M. C., Casse F., Chippaux M., Lepelletier M. Genetic analysis of mutants of Salmonella typhimurium deficient in formate dehydrogenase activity. Mol Gen Genet. 1973;120(4):337–340. doi: 10.1007/BF00268147. [DOI] [PubMed] [Google Scholar]
  253. Pascal M. C., Chippaux M., Abou-Jaoudé A., Blaschkowski H. P., Knappe J. Mutants of Escherichia coli K12 with defects in anaerobic pyruvate metabolism. J Gen Microbiol. 1981 May;124(1):35–42. doi: 10.1099/00221287-124-1-35. [DOI] [PubMed] [Google Scholar]
  254. Pascal M. C., Chippaux M. Involvement of a gene of the chl E locus in the regulation of the nitrate reductase operon. Mol Gen Genet. 1982;185(2):334–338. doi: 10.1007/BF00330808. [DOI] [PubMed] [Google Scholar]
  255. Patrick J. M., Dobrogosz W. J. The effect of cyclic AMP on anaerobic growth of Escherichia coli. Biochem Biophys Res Commun. 1973 Sep 18;54(2):555–561. doi: 10.1016/0006-291x(73)91458-7. [DOI] [PubMed] [Google Scholar]
  256. Paveglio M. T., Tang J. S., Unger R. E., Barrett E. L. Formate-nitrate respiration in Salmonella typhimurium: studies of two rha-linked fdn genes. J Bacteriol. 1988 Jan;170(1):213–217. doi: 10.1128/jb.170.1.213-217.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  257. Pecher A., Blaschkowski H. P., Knappe K., Böck A. Expression of pyruvate formate-lyase of Escherichia coli from the cloned structural gene. Arch Microbiol. 1982 Oct;132(4):365–371. doi: 10.1007/BF00413390. [DOI] [PubMed] [Google Scholar]
  258. Pecher A., Zinoni F., Böck A. The seleno-polypeptide of formic dehydrogenase (formate hydrogen-lyase linked) from Escherichia coli: genetic analysis. Arch Microbiol. 1985 May;141(4):359–363. doi: 10.1007/BF00428850. [DOI] [PubMed] [Google Scholar]
  259. Pecher A., Zinoni F., Jatisatienr C., Wirth R., Hennecke H., Böck A. On the redox control of synthesis of anaerobically induced enzymes in enterobacteriaceae. Arch Microbiol. 1983 Nov;136(2):131–136. doi: 10.1007/BF00404787. [DOI] [PubMed] [Google Scholar]
  260. Peterkofsky A., Gazdar C. Escherichia coli adenylate cyclase complex: regulation by the proton electrochemical gradient. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1099–1103. doi: 10.1073/pnas.76.3.1099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  261. Pichinoty F. Les nitrate-réductases bactériennes. I. Substrats, état particulaire et inhibiteurs de l'enzyme A. Arch Mikrobiol. 1969;68(1):51–64. [PubMed] [Google Scholar]
  262. Pichinoty F., Piéchaud M. Recherche des nitrate-réductases bactériennes A et B: méthodes. Ann Inst Pasteur (Paris) 1968 Jan;114(1):77–98. [PubMed] [Google Scholar]
  263. Pichinoty F., Puig J., Chippaux M., Bigliardi-Rouvier J., Gendre J. Recherches sur des mutants bactériens ayant perdu les activités catalytiques liées à la nitrate-réductase A. II. Comportement envers le chlorate et le chlorite. Ann Inst Pasteur (Paris) 1969 Apr;116(4):409–432. [PubMed] [Google Scholar]
  264. Piéchaud M., Pichinoty F., Azoulay E., Couchoud-Beaumont P., Gendre J. Recherches sur des mutants bactériens ayant perdu les activités catalytiques liées à la nitrate-réductase A. I. Description des méthodes d'isolement. Ann Inst Pasteur (Paris) 1969 Mar;116(3):276–287. [PubMed] [Google Scholar]
  265. Pope N. R., Cole J. A. Generation of a membrane potential by one of two independent pathways for nitrite reduction by Escherichia coli. J Gen Microbiol. 1982 Jan;128(1):219–222. doi: 10.1099/00221287-128-1-219. [DOI] [PubMed] [Google Scholar]
  266. Pope N. R., Cole J. A. Pyruvate and ethanol as electron donors for nitrite reduction by Escherichia coli K12. J Gen Microbiol. 1984 May;130(5):1279–1284. doi: 10.1099/00221287-130-5-1279. [DOI] [PubMed] [Google Scholar]
  267. Puig J., Azoulay E., Gendre J., Richard E. Etude génétique des mutants de la région chl A chez l'Escherichia coli k12. C R Acad Sci Hebd Seances Acad Sci D. 1969 Jan 6;268(1):183–184. [PubMed] [Google Scholar]
  268. Puig J., Azoulay E., Pichinoty F., Gendre J. Genetic mapping of the chl C gene of the nitrate reductase A system in Escherichia coli K12. Biochem Biophys Res Commun. 1969 Jun 6;35(5):659–662. doi: 10.1016/0006-291x(69)90455-0. [DOI] [PubMed] [Google Scholar]
  269. Quastel J. H., Stephenson M., Whetham M. D. Some Reactions of Resting Bacteria in Relation to Anaerobic Growth. Biochem J. 1925;19(2):304–317. doi: 10.1042/bj0190304. [DOI] [PMC free article] [PubMed] [Google Scholar]
  270. Quastel J. H., Wooldridge W. R. Reduction potential, energy exchange and cell growth: Experiments with B. coli. Biochem J. 1929;23(1):115–137. doi: 10.1042/bj0230115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  271. Raibaud O., Schwartz M. Positive control of transcription initiation in bacteria. Annu Rev Genet. 1984;18:173–206. doi: 10.1146/annurev.ge.18.120184.001133. [DOI] [PubMed] [Google Scholar]
  272. Reddy P., Miller D., Peterkofsky A. Stimulation of Escherichia coli adenylate cyclase activity by elongation factor Tu, a GTP-binding protein essential for protein synthesis. J Biol Chem. 1986 Sep 5;261(25):11448–11451. [PubMed] [Google Scholar]
  273. Reiss J., Kleinhofs A., Klingmüller W. Cloning of seven differently complementing DNA fragments with chl functions from Escherichia coli K12. Mol Gen Genet. 1987 Feb;206(2):352–355. doi: 10.1007/BF00333594. [DOI] [PubMed] [Google Scholar]
  274. Riet J van't, Knook D. L., Planta R. J. The role of cytochrome b 1 in nitrate assimilation and nitrate respiration in Klebsiella aerogenes. FEBS Lett. 1972 Jun 1;23(1):44–46. doi: 10.1016/0014-5793(72)80280-1. [DOI] [PubMed] [Google Scholar]
  275. Riet J van't The participation of cytochromes in the process of nitrate respiration in klesbsiella (Aerobacter) aerogenes. Biochim Biophys Acta. 1973 Jan 18;292(1):237–245. doi: 10.1016/0005-2728(73)90268-5. [DOI] [PubMed] [Google Scholar]
  276. Riley M., Anilionis A. Evolution of the bacterial genome. Annu Rev Microbiol. 1978;32:519–560. doi: 10.1146/annurev.mi.32.100178.002511. [DOI] [PubMed] [Google Scholar]
  277. Riviere C., Giordano G., Pommier J., Azoulay E. Membrane reconstitution in chl-r mutants of Escherichia coli K 12. VIII. Purification and properties of the FA factor, the product of the chl B gene. Biochim Biophys Acta. 1975 May 6;389(2):219–235. doi: 10.1016/0005-2736(75)90317-x. [DOI] [PubMed] [Google Scholar]
  278. Rondeau S. S., Hsu P. Y., DeMoss J. A. Construction in vitro of a cloned nar operon from Escherichia coli. J Bacteriol. 1984 Jul;159(1):159–166. doi: 10.1128/jb.159.1.159-166.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  279. Ruiz-Herrera J., DeMoss J. A. Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction. J Bacteriol. 1969 Sep;99(3):720–729. doi: 10.1128/jb.99.3.720-729.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  280. Ruiz-Herrera J., Salas-Vargas I. Regulation of nitrate reductase at the transcriptional and translational levels in Escherichia coli. Biochim Biophys Acta. 1976 Apr 2;425(4):492–501. doi: 10.1016/0005-2787(76)90013-7. [DOI] [PubMed] [Google Scholar]
  281. Ruiz-Herrera J., Showe M. K., DeMoss J. A. Nitrate reductase complex of Escherichia coli K-12: isolation and characterization of mutants unable to reduce nitrate. J Bacteriol. 1969 Mar;97(3):1291–1297. doi: 10.1128/jb.97.3.1291-1297.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  282. Ruíz-Herrera J., Alvarez A., Figueroa I. Solubilization and properties of formate dehydrogenases from the membrane of Escherichia coli. Biochim Biophys Acta. 1972 Dec 7;289(2):254–261. doi: 10.1016/0005-2744(72)90075-7. [DOI] [PubMed] [Google Scholar]
  283. Sanderson K. E. Genetic relatedness in the family Enterobacteriaceae. Annu Rev Microbiol. 1976;30:327–349. doi: 10.1146/annurev.mi.30.100176.001551. [DOI] [PubMed] [Google Scholar]
  284. Sankar P., Lee J. H., Shanmugam K. T. Cloning of hydrogenase genes and fine structure analysis of an operon essential for H2 metabolism in Escherichia coli. J Bacteriol. 1985 Apr;162(1):353–360. doi: 10.1128/jb.162.1.353-360.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  285. Saracino L., Violet M., Boxer D. H., Giordano G. Activation in vitro of respiratory nitrate reductase of Escherichia coli K12 grown in the presence of tungstate. Involvement of molybdenum cofactor. Eur J Biochem. 1986 Aug 1;158(3):483–490. doi: 10.1111/j.1432-1033.1986.tb09780.x. [DOI] [PubMed] [Google Scholar]
  286. Satoh T., Hom S. S., Shanmugam K. T. Production of nitrous oxide from nitrite in Klebsiella pneumoniae: mutants altered in nitrogen metabolism. J Bacteriol. 1983 Aug;155(2):454–458. doi: 10.1128/jb.155.2.454-458.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  287. Sawers R. G., Ballantine S. P., Boxer D. H. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J Bacteriol. 1985 Dec;164(3):1324–1331. doi: 10.1128/jb.164.3.1324-1331.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  288. Sawers R. G., Boxer D. H. Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12. Eur J Biochem. 1986 Apr 15;156(2):265–275. doi: 10.1111/j.1432-1033.1986.tb09577.x. [DOI] [PubMed] [Google Scholar]
  289. Sawers R. G., Jamieson D. J., Higgins C. F., Boxer D. H. Characterization and physiological roles of membrane-bound hydrogenase isoenzymes from Salmonella typhimurium. J Bacteriol. 1986 Oct;168(1):398–404. doi: 10.1128/jb.168.1.398-404.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  290. Sawers R. G., Zehelein E., Böck A. Two-dimensional gel electrophoretic analysis of Escherichia coli proteins: influence of various anaerobic growth conditions and the fnr gene product on cellular protein composition. Arch Microbiol. 1988 Jan;149(3):240–244. doi: 10.1007/BF00422011. [DOI] [PubMed] [Google Scholar]
  291. Schnaitman C. A. Alteration of membrane proteins in a chlorate-resistant mutant of Escherichia coli. Biochem Biophys Res Commun. 1969 Sep 24;37(1):1–5. doi: 10.1016/0006-291x(69)90871-7. [DOI] [PubMed] [Google Scholar]
  292. Schweizer H., Larson T. J. Cloning and characterization of the aerobic sn-glycerol-3-phosphate dehydrogenase structural gene glpD of Escherichia coli K-12. J Bacteriol. 1987 Feb;169(2):507–513. doi: 10.1128/jb.169.2.507-513.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  293. Scott R. H., DeMoss J. A. Formation of the formate-nitrate electron transport pathway from inactive components in Escherichia coli. J Bacteriol. 1976 Apr;126(1):478–486. doi: 10.1128/jb.126.1.478-486.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  294. Scott R. H., Sperl G. T., DeMoss J. A. In vitro incorporation of molybdate into demolybdoproteins in Escherichia coli. J Bacteriol. 1979 Feb;137(2):719–726. doi: 10.1128/jb.137.2.719-726.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  295. Shah V. K., Ugalde R. A., Imperial J., Brill W. J. Molybdenum in nitrogenase. Annu Rev Biochem. 1984;53:231–257. doi: 10.1146/annurev.bi.53.070184.001311. [DOI] [PubMed] [Google Scholar]
  296. Shaw D. J., Guest J. R. Amplification and product identification of the fnr gene of Escherichia coli. J Gen Microbiol. 1982 Oct;128(10):2221–2228. doi: 10.1099/00221287-128-10-2221. [DOI] [PubMed] [Google Scholar]
  297. Shaw D. J., Guest J. R. Molecular cloning of the fnr gene of Escherichia coli K12. Mol Gen Genet. 1981;181(1):95–100. doi: 10.1007/BF00339011. [DOI] [PubMed] [Google Scholar]
  298. Shaw D. J., Guest J. R. Nucleotide sequence of the fnr gene and primary structure of the Enr protein of Escherichia coli. Nucleic Acids Res. 1982 Oct 11;10(19):6119–6130. doi: 10.1093/nar/10.19.6119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  299. Shaw D. J., Rice D. W., Guest J. R. Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. J Mol Biol. 1983 May 15;166(2):241–247. doi: 10.1016/s0022-2836(83)80011-4. [DOI] [PubMed] [Google Scholar]
  300. Showe M. K., DeMoss J. A. Localization and regulation of synthesis of nitrate reductase in Escherichia coli. J Bacteriol. 1968 Apr;95(4):1305–1313. doi: 10.1128/jb.95.4.1305-1313.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  301. Shum A. C., Murphy J. C. Effects of selenium compounds on formate metabolism and coincidence of selenium-75 incorporation and formic dehydrogenase activity in cell-free preparations of Escherichia coli. J Bacteriol. 1972 Apr;110(1):447–449. doi: 10.1128/jb.110.1.447-449.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  302. Silvestro A., Pommier J., Giordano G. Molybdenum cofactor: a compound in the in vitro activation of both nitrate reductase and trimethylamine-N-oxide reductase activities in Escherichia coli K12. Biochim Biophys Acta. 1986 Aug 15;872(3):243–252. doi: 10.1016/0167-4838(86)90277-3. [DOI] [PubMed] [Google Scholar]
  303. Simoni R. D., Shallenberger M. K. Coupling of energy to active transport of amino acids in Escherichia coli. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2663–2667. doi: 10.1073/pnas.69.9.2663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  304. Singer S. J., Nicolson G. L. The fluid mosaic model of the structure of cell membranes. Science. 1972 Feb 18;175(4023):720–731. doi: 10.1126/science.175.4023.720. [DOI] [PubMed] [Google Scholar]
  305. Smith M. S. Nitrous oxide production by Escherichia coli is correlated with nitrate reductase activity. Appl Environ Microbiol. 1983 May;45(5):1545–1547. doi: 10.1128/aem.45.5.1545-1547.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  306. Smith M. W., Neidhardt F. C. 2-Oxoacid dehydrogenase complexes of Escherichia coli: cellular amounts and patterns of synthesis. J Bacteriol. 1983 Oct;156(1):81–88. doi: 10.1128/jb.156.1.81-88.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  307. Smith M. W., Neidhardt F. C. Proteins induced by aerobiosis in Escherichia coli. J Bacteriol. 1983 Apr;154(1):344–350. doi: 10.1128/jb.154.1.344-350.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  308. Smith M. W., Neidhardt F. C. Proteins induced by anaerobiosis in Escherichia coli. J Bacteriol. 1983 Apr;154(1):336–343. doi: 10.1128/jb.154.1.336-343.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  309. Sodergren E. J., DeMoss J. A. narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes. J Bacteriol. 1988 Apr;170(4):1721–1729. doi: 10.1128/jb.170.4.1721-1729.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  310. Spencer M. E., Guest J. R. Isolation and properties of fumarate reductase mutants of Escherichia coli. J Bacteriol. 1973 May;114(2):563–570. doi: 10.1128/jb.114.2.563-570.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  311. Spencer M. E., Guest J. R. Regulation of citric acid cycle genes in facultative bacteria. Microbiol Sci. 1987 Jun;4(6):164–168. [PubMed] [Google Scholar]
  312. Spencer M. E., Guest J. R. Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli. Mol Gen Genet. 1985;200(1):145–154. doi: 10.1007/BF00383328. [DOI] [PubMed] [Google Scholar]
  313. Sperl G. T., DeMoss J. A. chlD gene function in molybdate activation of nitrate reductase. J Bacteriol. 1975 Jun;122(3):1230–1238. doi: 10.1128/jb.122.3.1230-1238.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  314. Spiro S., Guest J. R. Activation of the lac operon of Escherichia coli by a mutant FNR protein. Mol Microbiol. 1987 Jul;1(1):53–58. doi: 10.1111/j.1365-2958.1987.tb00526.x. [DOI] [PubMed] [Google Scholar]
  315. Spiro S., Guest J. R. Regulation and over-expression of the fnr gene of Escherichia coli. J Gen Microbiol. 1987 Dec;133(12):3279–3288. doi: 10.1099/00221287-133-12-3279. [DOI] [PubMed] [Google Scholar]
  316. Stadtman T. C. Some selenium-dependent biochemical processes. Adv Enzymol Relat Areas Mol Biol. 1979;48:1–28. doi: 10.1002/9780470122938.ch1. [DOI] [PubMed] [Google Scholar]
  317. Stewart V., MacGregor C. H. Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci. J Bacteriol. 1982 Aug;151(2):788–799. doi: 10.1128/jb.151.2.788-799.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  318. Stewart V., Parales J., Jr Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12. J Bacteriol. 1988 Apr;170(4):1589–1597. doi: 10.1128/jb.170.4.1589-1597.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  319. Stewart V. Requirement of Fnr and NarL functions for nitrate reductase expression in Escherichia coli K-12. J Bacteriol. 1982 Sep;151(3):1320–1325. doi: 10.1128/jb.151.3.1320-1325.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  320. Stickland L. H. The reduction of nitrates by Bact. coli. Biochem J. 1931;25(5):1543–1554. doi: 10.1042/bj0251543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  321. Stouthamer A. H., Bettenhausen C., van Hartingsveldt J., Riet J van't, Planta R. J. Nitrate reduction in aerobacter aerogenes. 3. Nitrate reduction, chlorate resistance and formate metabolism in mutant strains. Arch Mikrobiol. 1967;58(3):228–247. doi: 10.1007/BF00408806. [DOI] [PubMed] [Google Scholar]
  322. Stouthamer A. H., Bettenhaussen C. W. Mapping of a gene causing resistance to chlorate in Salmonella typhimurium. Antonie Van Leeuwenhoek. 1970;36(4):555–565. doi: 10.1007/BF02069058. [DOI] [PubMed] [Google Scholar]
  323. Stouthamer A. H., Bettenhaussen C. Influence of hydrogen acceptors on growth and energy production of Proteus mirabilis. Antonie Van Leeuwenhoek. 1972;38(1):81–90. doi: 10.1007/BF02328079. [DOI] [PubMed] [Google Scholar]
  324. Stouthamer A. H., Bettenhaussen C. Utilization of energy for growth and maintenance in continuous and batch cultures of microorganisms. A reevaluation of the method for the determination of ATP production by measuring molar growth yields. Biochim Biophys Acta. 1973 Feb 12;301(1):53–70. doi: 10.1016/0304-4173(73)90012-8. [DOI] [PubMed] [Google Scholar]
  325. Stouthamer A. H. Biochemistry and genetics of nitrate reductase in bacteria. Adv Microb Physiol. 1976;14(11):315–375. doi: 10.1016/s0065-2911(08)60230-1. [DOI] [PubMed] [Google Scholar]
  326. Stouthamer A. H. Nitrate reduction in Aerobacter aerogenes. I. Isolation and properties of mutant strains blocked in nitrate assimilation and resistant against chlorate. Arch Mikrobiol. 1967 Feb 1;56(1):68–75. [PubMed] [Google Scholar]
  327. Stouthamer A. H. Nitrate reduction in Aerobacter aerogenes. II. Characterization of mutants blocked in the reduction of nitrate and chlorate. Arch Mikrobiol. 1967 Feb 1;56(1):76–80. [PubMed] [Google Scholar]
  328. Stouthamer A. H., Pietersma K. Deletion-mapping of resistance against chlorate in Klebsiella aerogenes. Mol Gen Genet. 1970;106(2):174–179. doi: 10.1007/BF00323836. [DOI] [PubMed] [Google Scholar]
  329. Strauch K. L., Lenk J. B., Gamble B. L., Miller C. G. Oxygen regulation in Salmonella typhimurium. J Bacteriol. 1985 Feb;161(2):673–680. doi: 10.1128/jb.161.2.673-680.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  330. Streicher S. L., Shanmugam K. T., Ausubel F., Morandi C., Goldberg R. B. Regulation of nitrogen fixation in Klebsiella pneumoniae: evidence for a role of glutamine synthetase as a regulator of nitrogenase synthesis. J Bacteriol. 1974 Nov;120(2):815–821. doi: 10.1128/jb.120.2.815-821.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  331. Sutherland P., McAlister-Henn L. Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase. J Bacteriol. 1985 Sep;163(3):1074–1079. doi: 10.1128/jb.163.3.1074-1079.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  332. Synthesis and sideedness of membrane-bound respiratory nitrate reductase (EC1.7.99.4) in Escherichia coli lacking cytochromes. Biochem J. 1975 May;148(2):329–333. [PMC free article] [PubMed] [Google Scholar]
  333. Sánchez Crispín J. A., Dubourdieu M., Chippaux M. Localization and characterization of cytochromes from membrane vesicles of Escherichia coli K-12 grown in anaerobiosis with nitrate. Biochim Biophys Acta. 1979 Aug 14;547(2):198–210. doi: 10.1016/0005-2728(79)90003-3. [DOI] [PubMed] [Google Scholar]
  334. TANIGUCHI S., ITAGAKI E. Nitrate reductase of nitrate respiration type from E. coli. I. Solubilization and purification from the particulate system with molecular characterization as a metalloprotein. Biochim Biophys Acta. 1960 Nov 4;44:263–279. doi: 10.1016/0006-3002(60)91562-6. [DOI] [PubMed] [Google Scholar]
  335. Teizeira de Mattos M. J., Tempest D. W. Metabolic and energetic aspects of the growth of Klebsiella aerogenes NCTC 418 on glucose in anaerobic chemostat culture. Arch Microbiol. 1983 Jan;134(1):80–85. doi: 10.1007/BF00429412. [DOI] [PubMed] [Google Scholar]
  336. Tempest D. W., Neijssel O. M. The status of YATP and maintenance energy as biologically interpretable phenomena. Annu Rev Microbiol. 1984;38:459–486. doi: 10.1146/annurev.mi.38.100184.002331. [DOI] [PubMed] [Google Scholar]
  337. Thayer J. R., Huffaker R. C. Kinetic evaluation, using 13N, reveals two assimilatory nitrate transport systems in Klebsiella pneumoniae. J Bacteriol. 1982 Jan;149(1):198–202. doi: 10.1128/jb.149.1.198-202.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  338. Thomas A. D., Doelle H. W., Westwood A. W., Gordon G. L. Effect of oxygen on several enzymes involved in the aerobic and anaerobic utilization of glucose in Escherichia coli. J Bacteriol. 1972 Dec;112(3):1099–1105. doi: 10.1128/jb.112.3.1099-1105.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  339. Unden G., Duchene A. On the role of cyclic AMP and the Fnr protein in Escherichia coli growing anaerobically. Arch Microbiol. 1987 Mar;147(2):195–200. doi: 10.1007/BF00415284. [DOI] [PubMed] [Google Scholar]
  340. Unden G., Guest J. R. Isolation and characterization of the Fnr protein, the transcriptional regulator of anaerobic electron transport in Escherichia coli. Eur J Biochem. 1985 Jan 2;146(1):193–199. doi: 10.1111/j.1432-1033.1985.tb08638.x. [DOI] [PubMed] [Google Scholar]
  341. Van 't Riet J., Planta R. J. Purification, structure and properties of the respiratory nitrate reductase of Klebsiella aerogenes. Biochim Biophys Acta. 1975 Jan 30;379(1):81–94. doi: 10.1016/0005-2795(75)90010-0. [DOI] [PubMed] [Google Scholar]
  342. Van Wielink J. E., Reijnders W. N., Van Spanning R. J., Oltmann L. F., Stouthamer A. H. The functional localization of cytochromes b in the respiratory chain of anaerobically grown Proteus mirabilis. Antonie Van Leeuwenhoek. 1986;52(2):105–116. doi: 10.1007/BF00429313. [DOI] [PubMed] [Google Scholar]
  343. Van der Beek E. G., Oltmann L. F., Stouthamer A. H. Fumarate reduction in Proteus mirabilis. Arch Microbiol. 1976 Nov 2;110(23):195–206. doi: 10.1007/BF00690228. [DOI] [PubMed] [Google Scholar]
  344. Vega J. M., Guerrero M. G., Leadbetter E., Losada M. Reduced nicotinamide-adenine dinucleotide-nitrite reductase from Azotobacter chroococcum. Biochem J. 1973 Aug;133(4):701–708. doi: 10.1042/bj1330701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  345. Venables W. A. Genetic studies with nitrate reductase-less mutants of Escherichia coli. I. Fine structure analysis of the narA, narB and narE loci. Mol Gen Genet. 1972;114(3):223–231. doi: 10.1007/BF01788891. [DOI] [PubMed] [Google Scholar]
  346. Venables W. A., Guest J. R. Transduction of nitrate reductase loci of Escherichia coli by phages P-1 and lambda. Mol Gen Genet. 1968;103(2):127–140. doi: 10.1007/BF00427140. [DOI] [PubMed] [Google Scholar]
  347. Vincent S. P., Bray R. C. Electron-paramagnetic-resonance studies on nitrate reductase from Escherichia coli K12. Biochem J. 1978 Jun 1;171(3):639–647. doi: 10.1042/bj1710639. [DOI] [PMC free article] [PubMed] [Google Scholar]
  348. Vincent S. P. Oxidation--reduction potentials of molybdenum and iron--sulphur centres in nitrate reductase from Escherichia coli. Biochem J. 1979 Feb 1;177(2):757–759. doi: 10.1042/bj1770757. [DOI] [PMC free article] [PubMed] [Google Scholar]
  349. Wahl R. C., Hageman R. V., Rajagopalan K. V. The relationship of Mo, molybdopterin, and the cyanolyzable sulfur in the Mo cofactor. Arch Biochem Biophys. 1984 Apr;230(1):264–273. doi: 10.1016/0003-9861(84)90107-3. [DOI] [PubMed] [Google Scholar]
  350. Wallace B. J., Young I. G. Aerobic respiration in mutants of Escherichia coli accumulating quinone analogues of ubiquinone. Biochim Biophys Acta. 1977 Jul 7;461(1):75–83. doi: 10.1016/0005-2728(77)90070-6. [DOI] [PubMed] [Google Scholar]
  351. Wallace B. J., Young I. G. Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA- menA- double quinone mutant. Biochim Biophys Acta. 1977 Jul 7;461(1):84–100. doi: 10.1016/0005-2728(77)90071-8. [DOI] [PubMed] [Google Scholar]
  352. Waugh R., Boxer D. H. Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity. Biochimie. 1986 Jan;68(1):157–166. doi: 10.1016/s0300-9084(86)81080-x. [DOI] [PubMed] [Google Scholar]
  353. Weber I. T., Gilliland G. L., Harman J. G., Peterkofsky A. Crystal structure of a cyclic AMP-independent mutant of catabolite gene activator protein. J Biol Chem. 1987 Apr 25;262(12):5630–5636. [PubMed] [Google Scholar]
  354. Wientjes F. B., Kolk A. H., Nanninga N., Van T'Riet J. Respiratory nitrate reductase: its localization in the cytoplasmic membrane of Klebsiella aerogenes and Bacillus licheniformis. Eur J Biochem. 1979 Mar 15;95(1):61–67. doi: 10.1111/j.1432-1033.1979.tb12939.x. [DOI] [PubMed] [Google Scholar]
  355. Wimpenny J. W., Cole J. A. The regulation of metabolism in facultative bacteria. 3. The effect of nitrate. Biochim Biophys Acta. 1967 Oct 9;148(1):233–242. doi: 10.1016/0304-4165(67)90298-x. [DOI] [PubMed] [Google Scholar]
  356. Wimpenny J. W., Necklen D. K. The redox environment and microbial physiology. I. The transition from anaerobiosis to aerobiosis in continuous cultures of facultative anaerobes. Biochim Biophys Acta. 1971 Dec 7;253(2):352–359. doi: 10.1016/0005-2728(71)90039-9. [DOI] [PubMed] [Google Scholar]
  357. Wimpenny J. W. The effect of Eh on regulatory processes in facultative anaerobes. Biotechnol Bioeng. 1969 Jul;11(4):623–629. doi: 10.1002/bit.260110409. [DOI] [PubMed] [Google Scholar]
  358. Wimpenny J. W., Warmsley A. M. The effect of nitrate on Krebs cycle enzymes in various bacteria. Biochim Biophys Acta. 1968 Mar 11;156(2):297–303. doi: 10.1016/0304-4165(68)90258-4. [DOI] [PubMed] [Google Scholar]
  359. Wu L. F., Mandrand-Berthelot M. A. Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity. Biochimie. 1986 Jan;68(1):167–179. doi: 10.1016/s0300-9084(86)81081-1. [DOI] [PubMed] [Google Scholar]
  360. Wu L. F., Mandrand-Berthelot M. A. Regulation of the fdhF gene encoding the selenopolypeptide for benzyl viologen-linked formate dehydrogenase in Escherichia coli. Mol Gen Genet. 1987 Aug;209(1):129–134. doi: 10.1007/BF00329847. [DOI] [PubMed] [Google Scholar]
  361. Yamamoto I., Ishimoto M. Anaerobic growth of Escherichia coli on formate by reduction of nitrate, fumarate, and trimethylamine N-oxide. Z Allg Mikrobiol. 1977;17(3):235–242. doi: 10.1002/jobm.3630170309. [DOI] [PubMed] [Google Scholar]
  362. Yamamoto I., Ishimoto M. Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. J Biochem. 1975 Aug;78(2):307–315. doi: 10.1093/oxfordjournals.jbchem.a130909. [DOI] [PubMed] [Google Scholar]
  363. Yamamoto N., Droffner M. L. Mechanisms determining aerobic or anaerobic growth in the facultative anaerobe Salmonella typhimurium. Proc Natl Acad Sci U S A. 1985 Apr;82(7):2077–2081. doi: 10.1073/pnas.82.7.2077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  364. Yang F. D., Yu L., Yu C. A., Lorence R. M., Gennis R. B. Use of an azido-ubiquinone derivative to identify subunit I as the ubiquinol binding site of the cytochrome d terminal oxidase complex of Escherichia coli. J Biol Chem. 1986 Nov 15;261(32):14987–14990. [PubMed] [Google Scholar]
  365. Yerkes J. H., Casson L. P., Honkanen A. K., Walker G. C. Anaerobiosis induces expression of ant, a new Escherichia coli locus with a role in anaerobic electron transport. J Bacteriol. 1984 Apr;158(1):180–186. doi: 10.1128/jb.158.1.180-186.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  366. Zinoni F., Beier A., Pecher A., Wirth R., Böck A. Regulation of the synthesis of hydrogenase (formate hydrogen-lyase linked) of E. coli. Arch Microbiol. 1984 Nov;139(4):299–304. doi: 10.1007/BF00408370. [DOI] [PubMed] [Google Scholar]
  367. Zinoni F., Birkmann A., Leinfelder W., Böck A. Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc Natl Acad Sci U S A. 1987 May;84(10):3156–3160. doi: 10.1073/pnas.84.10.3156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  368. Zinoni F., Birkmann A., Stadtman T. C., Böck A. Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4650–4654. doi: 10.1073/pnas.83.13.4650. [DOI] [PMC free article] [PubMed] [Google Scholar]
  369. de Crombrugghe B., Busby S., Buc H. Cyclic AMP receptor protein: role in transcription activation. Science. 1984 May 25;224(4651):831–838. doi: 10.1126/science.6372090. [DOI] [PubMed] [Google Scholar]
  370. del Campillo-Campbell A., Campbell A. Molybdenum cofactor requirement for biotin sulfoxide reduction in Escherichia coli. J Bacteriol. 1982 Feb;149(2):469–478. doi: 10.1128/jb.149.2.469-478.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  371. van Riet J., van Ed J. H., Wever R., van Gelder B. F., Planta R. J. Characterization of the respiratory nitrate reductase of Klebsiella aerogenes as a molybdenum-containing iron-sulfur enzyme. Biochim Biophys Acta. 1975 Oct 20;405(2):306–317. doi: 10.1016/0005-2795(75)90096-3. [DOI] [PubMed] [Google Scholar]
  372. van Wielink J. E., Reijnders W. N., Oltmann L. F., Leeuwerik F. J., Stouthamer A. H. The membrane-bound b and c-type cytochromes of Proteus mirabilis grown under different conditions. Characterization by means of coupled spectrum deconvolution and potentiometric analysis. Arch Microbiol. 1983 Feb;134(2):118–122. doi: 10.1007/BF00407943. [DOI] [PubMed] [Google Scholar]
  373. van der Plas J., Hellingwerf K. J., Seijen H. G., Guest J. R., Weiner J. H., Konings W. N. Identification and localization of enzymes of the fumarate reductase and nitrate respiration systems of escherichia coli by crossed immunoelectrophoresis. J Bacteriol. 1983 Feb;153(2):1027–1037. doi: 10.1128/jb.153.2.1027-1037.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Microbiological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES