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. 1981 Dec;45(4):542–555. doi: 10.1128/mr.45.4.542-555.1981

Succinate dehydrogenase--a comparative review.

L Hederstedt, L Rutberg
PMCID: PMC281527  PMID: 6799760

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Selected References

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  1. Ackrell B. A., Ball M. B., Kearney E. B. Peptides from complex II active in reconstitution of succinate-ubiquinone reductase. J Biol Chem. 1980 Apr 10;255(7):2761–2769. [PubMed] [Google Scholar]
  2. Ackrell B. A., Kearney E. B., Coles C. J., Singer T. P., Beinert H., Wan Y. P., Folkers K. Kinetics of the reoxidation of succinate dehydrogenase. Arch Biochem Biophys. 1977 Jul;182(1):107–117. doi: 10.1016/0003-9861(77)90288-0. [DOI] [PubMed] [Google Scholar]
  3. Ackrell B. A., Kearney E. B., Singer T. P. Mammalian succinate dehydrogenase. Methods Enzymol. 1978;53:466–483. doi: 10.1016/s0076-6879(78)53050-4. [DOI] [PubMed] [Google Scholar]
  4. Albracht S. P. The prosthetic groups in succinate dehydrogenase. Number and stoichiometry. Biochim Biophys Acta. 1980 Mar 14;612(1):11–28. doi: 10.1016/0005-2744(80)90274-0. [DOI] [PubMed] [Google Scholar]
  5. Ashraf J., Somasundaram T., Jayaraman J. Assembly of succinic dehydrogenase complex into mitochondrial membrane in yeast. Biochem Biophys Res Commun. 1980 Nov 17;97(1):263–269. doi: 10.1016/s0006-291x(80)80163-x. [DOI] [PubMed] [Google Scholar]
  6. Beinert H., Ackrell B. A., Vinogradov A. D., Kearney E. B., Singer T. P. Interrelations of reconstitution activity, reactions with electron acceptors, and iron-sulfur centers in succinate dehydrogenase. Arch Biochem Biophys. 1977 Jul;182(1):95–106. doi: 10.1016/0003-9861(77)90287-9. [DOI] [PubMed] [Google Scholar]
  7. Bruni A., Racker E. Resolution and reconstitution of the mitochondrial electron transport system. I. Reconstitution of the succinate-ubiquinone reductase. J Biol Chem. 1968 Mar 10;243(5):962–971. [PubMed] [Google Scholar]
  8. Capaldi R. A., Sweetland J., Merli A. Polypeptides in the succinate-coenzyme Q reductase segment of the respiratory chain. Biochemistry. 1977 Dec 27;16(26):5707–5710. doi: 10.1021/bi00645a009. [DOI] [PubMed] [Google Scholar]
  9. Capaldi R. A., Vanderkooi G. The low polarity of many membrane proteins. Proc Natl Acad Sci U S A. 1972 Apr;69(4):930–932. doi: 10.1073/pnas.69.4.930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Carls R. A., Hanson R. S. Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol. 1971 Jun;106(3):848–855. doi: 10.1128/jb.106.3.848-855.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Coles C. J., Holm R. H., Kurtz D. M., Jr, Orme-Johnson W. H., Rawlings J., Singer T. P., Wong G. B. Characterization of the iron-sulfur centers in succinate dehydrogenase. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3805–3808. doi: 10.1073/pnas.76.8.3805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Coles C. J., Singer T. P., White G. A., Thorn G. D. Studies on the binding of carboxin analogs to succinate dehydrogenase. J Biol Chem. 1978 Aug 25;253(16):5573–5578. [PubMed] [Google Scholar]
  13. Coles C. J., Tisdale H. D., Kenney W. C., Singer T. P. Studies on succinate dehydrogenase: XXI. Quaternary structure of succinate dehydrogenase. Physiol Chem Phys. 1972;4(4):301–316. [PubMed] [Google Scholar]
  14. Collins M. L., Salton M. R. Solubility characteristics of Micrococcus lysodeikticus membrane components in detergents and chaotropic salts analyzed by immunoelectrophoresis. Biochim Biophys Acta. 1979 May 3;553(1):40–53. doi: 10.1016/0005-2736(79)90029-4. [DOI] [PubMed] [Google Scholar]
  15. Creaghan I. T., Guest J. R. Amber mutants of the -ketoglutarate dehydrogenase gene of Escherichia coli K12. J Gen Microbiol. 1972 Jul;71(2):207–220. doi: 10.1099/00221287-71-2-207. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Cusanovich M. A., Kamen M. D. Light-induced electron transport in Chromatium strain D. I. Isolation and characterization of Chromatium chromatophores. Biochim Biophys Acta. 1968 Feb 12;153(2):376–396. doi: 10.1016/0005-2728(68)90082-0. [DOI] [PubMed] [Google Scholar]
  18. Davis K. A., Hatefi Y., Crawford I. P., Baltscheffsky H. Purification, molecular properties, and amino acid composition of the subunits of Rhodospirillum rubrum succinate dehydrogenase. Arch Biochem Biophys. 1977 Apr 30;180(2):459–464. doi: 10.1016/0003-9861(77)90060-1. [DOI] [PubMed] [Google Scholar]
  19. Davis K. A., Hatefi Y. Succinate dehydrogenase. I. Purification, molecular properties, and substructure. Biochemistry. 1971 Jun 22;10(13):2509–2516. doi: 10.1021/bi00789a014. [DOI] [PubMed] [Google Scholar]
  20. DePierre J. W., Ernster L. Enzyme topology of intracellular membranes. Annu Rev Biochem. 1977;46:201–262. doi: 10.1146/annurev.bi.46.070177.001221. [DOI] [PubMed] [Google Scholar]
  21. Edwards D. L., Belsole D. M., Guzik H. J., Unger B. W. Selection of succinic dehydrogenase mutants of Neurospora crassa. J Bacteriol. 1979 Feb;137(2):900–904. doi: 10.1128/jb.137.2.900-904.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Elferink M. G., Hellingwerf K. J., Michels P. A., Seÿen H. G., Konings W. N. Immunochemical analysis of membrane vesicles and chromatophoresis of Rhodopseudomonas sphaeroides by crossed immunoelectrophoresis. FEBS Lett. 1979 Nov 15;107(2):300–307. doi: 10.1016/0014-5793(79)80395-6. [DOI] [PubMed] [Google Scholar]
  23. Fortnagel P., Freese E. Analysis of sporulation mutants. II. Mutants blocked in the citric acid cycle. J Bacteriol. 1968 Apr;95(4):1431–1438. doi: 10.1128/jb.95.4.1431-1438.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Georgopoulos S. G., Alexandri E., Chrysayi M. Genetic evidence for the action of oxathiin and thiazole derivatives on the succinic dehydrogenase system of Ustilago maydis mitochondria. J Bacteriol. 1972 Jun;110(3):809–817. doi: 10.1128/jb.110.3.809-817.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Girdlestone J., Bisson R., Capaldi R. A. Interaction of succinate--ubiquinone reductase (complex II) with (arylazido)phospholipids. Biochemistry. 1981 Jan 6;20(1):152–156. doi: 10.1021/bi00504a025. [DOI] [PubMed] [Google Scholar]
  26. Gunatilleke I. A., Arst H. N., Jr, Scazzocchio C. Three genes determine the carboxin sensitivity of mitochondrial succinate oxidation in aspergillus nidulans. Genet Res. 1975 Dec;26(3):297–305. doi: 10.1017/s0016672300016098. [DOI] [PubMed] [Google Scholar]
  27. HIRSCH C. A., RASMINSKY M., DAVIS B. D., LIN E. C. A FUMARATE REDUCTASE IN ESCHERICHIA COLI DISTINCT FROM SUCCINATE DEHYDROGENASE. J Biol Chem. 1963 Nov;238:3770–3774. [PubMed] [Google Scholar]
  28. Hanstein W. G., Davis K. A., Ghalambor M. A., Hatefi Y. Succinate dehydrogenase. II. Enzymatic properties. Biochemistry. 1971 Jun 22;10(13):2517–2524. doi: 10.1021/bi00789a015. [DOI] [PubMed] [Google Scholar]
  29. Hatefi Y., Davis K. A., Baltscheffsky H., Baltscheffsky M., Johansson B. C. Isolation and properties of succinate dehydrogenase from Rhodospirillum rubrum. Arch Biochem Biophys. 1972 Oct;152(2):613–618. doi: 10.1016/0003-9861(72)90257-3. [DOI] [PubMed] [Google Scholar]
  30. Hatefi Y., Galante Y. M. Isolation of cytochrome b560 from complex II (succinateùbiquinone oxidoreductase) and its reconstitution with succinate dehydrogenase. J Biol Chem. 1980 Jun 25;255(12):5530–5537. [PubMed] [Google Scholar]
  31. Hatefi Y., Galante Y. M., Stiggall D. L., Ragan C. I. Proteins, polypeptides, prosthetic groups, and enzymic properties of complexes I, II, III, IV, and V of the mitochondrial oxidative phosphorylation system. Methods Enzymol. 1979;56:577–602. doi: 10.1016/0076-6879(79)56056-x. [DOI] [PubMed] [Google Scholar]
  32. Hatefi Y., Stiggall D. L. Preparation and properties of succinate: ubiquinone oxidoreductase (complex II). Methods Enzymol. 1978;53:21–27. doi: 10.1016/s0076-6879(78)53008-5. [DOI] [PubMed] [Google Scholar]
  33. Hederstedt L. Cytochrome b reducible by succinate in an isolated succinate dehydrogenase-cytochrome b complex from Bacillus subtilis membranes. J Bacteriol. 1980 Dec;144(3):933–940. doi: 10.1128/jb.144.3.933-940.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Hederstedt L., Holmgren E., Rutberg L. Characterization of a succinate dehydrogenase complex solubilized from the cytoplasmic membrane of Bacillus subtilis with the nonionic detergent Triton X-100. J Bacteriol. 1979 May;138(2):370–376. doi: 10.1128/jb.138.2.370-376.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Hederstedt L., Rutberg L. Biosynthesis and membrane binding of succinate dehydrogenase in Bacillus subtilis. J Bacteriol. 1980 Dec;144(3):941–951. doi: 10.1128/jb.144.3.941-951.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Hendler R. W., Burgess A. H. Fractionation of the electron-transport chain of Escherichia coli. Biochim Biophys Acta. 1974 Aug 23;357(2):215–230. doi: 10.1016/0005-2728(74)90062-0. [DOI] [PubMed] [Google Scholar]
  37. Hendler R. W., Burgess A. H. Respiration and protein synthesis in Escherichia coli membrane-envelope fragments. VI. Solubilization and characterization of the electron transport chain. J Cell Biol. 1972 Nov;55(2):266–281. doi: 10.1083/jcb.55.2.266. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Henner D. J., Hoch J. A. The Bacillus subtilis chromosome. Microbiol Rev. 1980 Mar;44(1):57–82. doi: 10.1128/mr.44.1.57-82.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Holmgren E., Hederstedt L., Rutberg L. Role of heme in synthesis and membrane binding of succinic dehydrogenase in Bacillus subtilis. J Bacteriol. 1979 May;138(2):377–382. doi: 10.1128/jb.138.2.377-382.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Ingledew W. J., Prince R. C. Thermodynamic resolution of the iron-sulfur centers of the succinic dehydrogenase of Rhodopseudomonas sphaeroides. Arch Biochem Biophys. 1977 Jan 15;178(1):303–307. doi: 10.1016/0003-9861(77)90195-3. [DOI] [PubMed] [Google Scholar]
  41. Ito J., Spizizen J. Increased rate of asporogenous mutations following treatment of Bacillus subtilis spores with ethyl methanesulfonate. Mutat Res. 1971 Sep;13(1):93–96. doi: 10.1016/0027-5107(71)90130-8. [DOI] [PubMed] [Google Scholar]
  42. KEILIN D., KING T. E. Reconstitution of the succinic oxidase system from soluble succinic dehydrogenase and a particulate cytochrome system preparation. Nature. 1958 May 31;181(4622):1520–1522. doi: 10.1038/1811520a0. [DOI] [PubMed] [Google Scholar]
  43. Kalra V. K., Murti C. R., Brodie A. F. Resolution and reconstitution of the succinoxidase pathway of Mycobacterium phlei. Arch Biochem Biophys. 1971 Dec;147(2):734–743. doi: 10.1016/0003-9861(71)90433-4. [DOI] [PubMed] [Google Scholar]
  44. Kasahara M., Anraku Y. Succinate dehydrogenase of Escherichia coli membrane vesicles. Activation and properties of the enzyme. J Biochem. 1974 Nov;76(5):959–966. [PubMed] [Google Scholar]
  45. Kenney W. C., Mowery P. C., Seng R. L., Singer T. P. Localization of the substrate and oxalacetate binding site of succinate dehydrogenase. J Biol Chem. 1976 Apr 25;251(8):2369–2373. [PubMed] [Google Scholar]
  46. Kim I. C., Bragg P. D. Some properties of the succinate dehydrogenase of Escherichia coli. Can J Biochem. 1971 Oct;49(10):1098–1104. doi: 10.1139/o71-159. [DOI] [PubMed] [Google Scholar]
  47. Klingenberg M. The ferricyanide method for elucidating the sidedness of membrane-bound dehydrogenases. Methods Enzymol. 1979;56:229–233. doi: 10.1016/0076-6879(79)56025-x. [DOI] [PubMed] [Google Scholar]
  48. Kok J D. E., Muller J. L., Slater E. C. EPR studies on the respiratory chain of wild-type Saccharomyces cerevisiae and mutants with a deficiency in succinate dehydrogenase. Biochim Biophys Acta. 1975 Jun 17;387(3):441–450. doi: 10.1016/0005-2728(75)90084-5. [DOI] [PubMed] [Google Scholar]
  49. Konings W. N. Localization of membrane proteins in membrane vesicles of Bacillus subtilis. Arch Biochem Biophys. 1975 Apr;167(2):570–580. doi: 10.1016/0003-9861(75)90500-7. [DOI] [PubMed] [Google Scholar]
  50. LARA F. J. The succinic dehydrogenase of Propionibacterium pentosaceum. Biochim Biophys Acta. 1959 Jun;33(2):565–567. doi: 10.1016/0006-3002(59)90153-2. [DOI] [PubMed] [Google Scholar]
  51. Lascelles J. Heme-deficient mutants of Staphylococcus aureus. Methods Enzymol. 1979;56:172–178. doi: 10.1016/0076-6879(79)56019-4. [DOI] [PubMed] [Google Scholar]
  52. Linder R., Salton M. R. Affinity chromatography of succinate dehydrogenase from the membranes of Micrococcus lysodeikticus. Prep Biochem. 1975;5(4):349–357. doi: 10.1080/00327487508061582. [DOI] [PubMed] [Google Scholar]
  53. MADSEN N. B. The oxidation of succinate in extracts of xanthomonas phaseoli. Can J Biochem Physiol. 1960 May;38:481–492. [PubMed] [Google Scholar]
  54. Mascarello J. T., Soderberg K., Scheffler I. E. Assignment of a gene for succinate dehydrogenase to human chromosome 1 by somatic cell hybridization. Cytogenet Cell Genet. 1980;28(1-2):121–135. doi: 10.1159/000131520. [DOI] [PubMed] [Google Scholar]
  55. Merli A., Capaldi R. A., Ackrell B. A., Kearney E. B. Arrangement of complex II (succinate-ubiguinone reductase) in the mitochondrial inner membrane. Biochemistry. 1979 Apr 17;18(8):1393–1400. doi: 10.1021/bi00575a001. [DOI] [PubMed] [Google Scholar]
  56. Mowery P. C., Steenkamp D. J., Ackrell A. C., Singer T. P., White G. A. Inhibition of mammalian succinate dehydrogenase by carboxins. Arch Biochem Biophys. 1977 Jan 30;178(2):495–506. doi: 10.1016/0003-9861(77)90220-x. [DOI] [PubMed] [Google Scholar]
  57. Nakayama N., Sugimoto I., Asahi T. Presence in Dry Pea Cotyledons of Soluble Succinate Dehydrogenase That Is Assembled into the Mitochondrial Inner Membrane during Seed Imbibition. Plant Physiol. 1980 Feb;65(2):229–233. doi: 10.1104/pp.65.2.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Oelze J. Proteins exposed at the surface of chromatophores of Rhodospirillum rubrum: the orientation of isolated chromatophores. Biochim Biophys Acta. 1978 Jun 2;509(3):450–461. doi: 10.1016/0005-2736(78)90239-0. [DOI] [PubMed] [Google Scholar]
  59. Ohnishi T., King T. E. EPR and other properties of succinate dehydrogenase. Methods Enzymol. 1978;53:483–495. doi: 10.1016/s0076-6879(78)53051-6. [DOI] [PubMed] [Google Scholar]
  60. Ohné M. Regulation of the dicarboxylic acid part of the citric acid cycle in Bacillus subtilis. J Bacteriol. 1975 Apr;122(1):224–234. doi: 10.1128/jb.122.1.224-234.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Ohné M., Rutberg B., Hoch J. A. Genetic and biochemical characterization of mutants of Bacillus subtilis defective in succinate dehydrogenase. J Bacteriol. 1973 Sep;115(3):738–745. doi: 10.1128/jb.115.3.738-745.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Owen P., Freer J. H. Factors influencing the activity of succinate dehydrogenase in membrane preparations from Micrococcus lysodeikticus. Biochem J. 1970 Nov;120(2):237–243. doi: 10.1042/bj1200237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Owen P., Kaback H. R. Antigenic architecture of membrane vesicles from Escherichia coli. Biochemistry. 1979 Apr 17;18(8):1422–1426. doi: 10.1021/bi00575a005. [DOI] [PubMed] [Google Scholar]
  64. Owen P., Salton M. R. Membrane asymmetry and expression of cell surface antigens of Micrococcus lysodeikticus established by crossed immunoelectrophoresis. J Bacteriol. 1977 Dec;132(3):974–978. doi: 10.1128/jb.132.3.974-985.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. PAPPENHEIMER A. M., Jr, HOWLAND J. L., MILLER P. A. Electron-transport systems in Corynebacterium diphtheriae. Biochim Biophys Acta. 1962 Oct 22;64:229–242. doi: 10.1016/0006-3002(62)90734-5. [DOI] [PubMed] [Google Scholar]
  66. Pollock J. J., Linder R., Salton M. R. Characterization of the membrane-bound succinic dehydrogenase of Micrococcus lysodeikticus. J Bacteriol. 1971 Jul;107(1):230–238. doi: 10.1128/jb.107.1.230-238.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Ramsay R. R., Ackrell B. A., Coles C. J., Singer T. P., White G. A., Thorn G. D. Reaction site of carboxanilides and of thenoyltrifluoroacetone in complex II. Proc Natl Acad Sci U S A. 1981 Feb;78(2):825–828. doi: 10.1073/pnas.78.2.825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Reddy T. L., Hendler R. W. Reconstitution of escherichia coli succinoxidase from soluble components. J Biol Chem. 1978 Nov 10;253(21):7972–7979. [PubMed] [Google Scholar]
  69. Righetti Piergiorgio, Cerletti Paolo. Molecular parameters of the beef heart succinate dehydrogenase. FEBS Lett. 1971 Mar 5;13(3):181–183. doi: 10.1016/0014-5793(71)80230-2. [DOI] [PubMed] [Google Scholar]
  70. Rutberg B., Hederstedt L., Holmgren E., Rutberg L. Characterization of succinic dehydrogenase mutants of Bacillus subtilis by crossed immunoelectrophoresis. J Bacteriol. 1978 Oct;136(1):304–311. doi: 10.1128/jb.136.1.304-311.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Rutberg B., Hoch J. A. Citric acid cycle: gene-enzyme relationships in Bacillus subtilis. J Bacteriol. 1970 Nov;104(2):826–833. doi: 10.1128/jb.104.2.826-833.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Ruíz-Herrera J., García L. G. Regulation of succinate dehydrogenase in Escherichia coli. J Gen Microbiol. 1972 Aug;72(1):29–35. doi: 10.1099/00221287-72-1-29. [DOI] [PubMed] [Google Scholar]
  73. Salerno J. C., Lim J., King T. E., Blum H., Ohnishi T. The spatial relationships and structure of the binuclear iron-sulfur clusters in succinate dehydrogenase. J Biol Chem. 1979 Jun 10;254(11):4828–4835. [PubMed] [Google Scholar]
  74. Singer T. P., Kearney E. B., Kenney W. C. Succinate dehydrogenase. Adv Enzymol Relat Areas Mol Biol. 1973;37:189–272. doi: 10.1002/9780470122822.ch4. [DOI] [PubMed] [Google Scholar]
  75. 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]
  76. Spencer M. E., Guest J. R. Proteins of the inner membrane of Escherichia coli: identification of succinate dehydrogenase by polyacrylamide gel electrophoresis with sdh amber mutants. J Bacteriol. 1974 Mar;117(3):947–953. doi: 10.1128/jb.117.3.947-953.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Takemoto J., Bachmann R. C. Orientation of chromatophores and spheroplast-derived membrane vesicles of Rhodopseudomonas sphaeroides: analysis by localization of enzyme activities. Arch Biochem Biophys. 1979 Jul;195(2):526–534. doi: 10.1016/0003-9861(79)90379-5. [DOI] [PubMed] [Google Scholar]
  78. Tanford C., Reynolds J. A. Characterization of membrane proteins in detergent solutions. Biochim Biophys Acta. 1976 Oct 26;457(2):133–170. doi: 10.1016/0304-4157(76)90009-5. [DOI] [PubMed] [Google Scholar]
  79. Tucker A. N., Lillich T. T. Effect of the systemic fungicide carboxin on electron transport function in membranes of Micrococcus denitrificans. Antimicrob Agents Chemother. 1974 Nov;6(5):572–578. doi: 10.1128/aac.6.5.572. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Ulrich J. T., Mathre D. E. Mode of action of oxathiin systemic fungicides. V. Effect on electron transport system of Ustilago maydis and Saccharomyces cerevisiae. J Bacteriol. 1972 May;110(2):628–632. doi: 10.1128/jb.110.2.628-632.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Vinogradov A. D., Ackrell B. A., Singer T. P. On the possible interrelations of the reactivity of soluble succinate dehydrogenase with ferricyanide, reconstitution activity, and the Hipip iron sulfur center. Biochem Biophys Res Commun. 1975 Nov 17;67(2):803–809. doi: 10.1016/0006-291x(75)90884-0. [DOI] [PubMed] [Google Scholar]
  82. Vinogradov A. D., Gavrikov V. G., Gavrikova E. V. Studies on the succinate dehydrogenating system. II. Reconstitution of succinate-ubiquinone reductase from the soluble components. Biochim Biophys Acta. 1980 Aug 5;592(1):13–27. doi: 10.1016/0005-2728(80)90110-3. [DOI] [PubMed] [Google Scholar]
  83. Vinogradov A. D., Goloveshkina V. G., Gavrikova E. V. The catalytic activity of soluble and membrane-bound succinate dehydrogenase. FEBS Lett. 1977 Feb 1;73(2):235–238. doi: 10.1016/0014-5793(77)80988-5. [DOI] [PubMed] [Google Scholar]
  84. Weiss H., Kolb H. J. Isolation of mitochondrial succinate: ubiquinone reductase, cytochrome c reductase and cytochrome c oxidase from Neurospora crassa using nonionic detergent. Eur J Biochem. 1979 Aug 15;99(1):139–149. doi: 10.1111/j.1432-1033.1979.tb13240.x. [DOI] [PubMed] [Google Scholar]
  85. Woods R. A., Sanders H. K., Briquet M., Foury F., Drysdale B. E., Mattoon J. R. Regulation of mitochondrial biogenesis: enzymatic changes in cytochrome-deficient yeast mutants requiring delta-aminolevulinic acid. J Biol Chem. 1975 Dec 10;250(23):9090–9098. [PubMed] [Google Scholar]
  86. Yoch D. C., Carithers R. P., Arnon D. I. Isolation and characterization of bound ion-sulfur proteins from bacterial photosynthetic membranes. I. Ferredoxins III and IV from Rhodospirillum rubrum chromatophores. J Biol Chem. 1977 Nov 10;252(21):7453–7460. [PubMed] [Google Scholar]
  87. Yu C. A., Yu L. Isolation and properties of a mitochondrial protein that converts succinate dehydrogenase into succinate-ubiquinone oxidoreductase. Biochemistry. 1980 Jul 22;19(15):3579–3585. doi: 10.1021/bi00556a025. [DOI] [PubMed] [Google Scholar]
  88. Yu L., Yu C. A. Interaction between succinate dehydrogenase and ubiquinone-binding protein from succinate-ubiquinone reductase. Biochim Biophys Acta. 1980 Nov 5;593(1):24–38. doi: 10.1016/0005-2728(80)90005-5. [DOI] [PubMed] [Google Scholar]

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