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. 1984 Jul;159(1):138–144. doi: 10.1128/jb.159.1.138-144.1984

Regulation by molecular oxygen and organic substrates of hydrogenase synthesis in Alcaligenes eutrophus.

G A Cangelosi, M L Wheelis
PMCID: PMC215604  PMID: 6376469

Abstract

Chemoautotrophic growth of Alcaligenes eutrophus 17707 is inhibited by 20% oxygen in the gas phase. Lowering the oxygen concentration to 4% results in chloramphenicol-sensitive derepression of soluble and membrane-bound hydrogenase activity (and of soluble hydrogenase antigen), showing that oxygen inhibition is due at least in part to repression of hydrogenase synthesis. Mutations resulting in derepression of hydrogenase activity (and antigen) under 25% oxygen (Ose-) mobilized with a self-transmissable plasmid which is already known to carry genes necessary for hydrogenase expression. Plasmid-borne mutations resulting in loss of soluble hydrogenase activity have no effect on the Ose phenotype, but chromosomal mutations resulting in reduction or loss of both hydrogenase activities cannot be made Ose-. The Ose- mutation does not alter the thermostability of either hydrogenase, and soluble hydrogenase in the mutant reacts with complete identity with that of the wild type, indicating that the Ose- phenotype does not result from structural alterations in either enzyme. Ose- mutants are also relieved of normal hydrogenase repression by organic substrates, which aggravates hydrogenase-mediated inhibition of heterotrophic growth by hydrogen. Regulation of hydrogenase in Ose- strains of A. eutrophus 17707 is nearly identical to that of wild-type A. eutrophus strains H1 and H16.

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Selected References

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

  1. Bowien B., Mayer F., Codd G. A., Schlegel H. G. Purification, some properties and quaternary structure of the D-ribulose 1,5-diphosphate carboxylase of Alcaligenes eutrophus. Arch Microbiol. 1976 Nov 2;110(23):157–166. doi: 10.1007/BF00690223. [DOI] [PubMed] [Google Scholar]
  2. Bowien B., Schlegel H. G. Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria. Annu Rev Microbiol. 1981;35:405–452. doi: 10.1146/annurev.mi.35.100181.002201. [DOI] [PubMed] [Google Scholar]
  3. Davis D. H., Stanier R. Y., Doudoroff M., Mandel M. Taxonomic studies on some gram negative polarly flagellated "hydrogen bacteria" and related species. Arch Mikrobiol. 1970;70(1):1–13. doi: 10.1007/BF00691056. [DOI] [PubMed] [Google Scholar]
  4. Dixon R. O. Hydrogenase in legume root nodule bacteroids: occurrence and properties. Arch Mikrobiol. 1972;85(3):193–201. doi: 10.1007/BF00408844. [DOI] [PubMed] [Google Scholar]
  5. Friedrich B., Hogrefe C., Schlegel H. G. Naturally occurring genetic transfer of hydrogen-oxidizing ability between strains of Alcaligenes eutrophus. J Bacteriol. 1981 Jul;147(1):198–205. doi: 10.1128/jb.147.1.198-205.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Friedrich B., Schlegel H. G. Aromatic amino acid biosynthesis in Alcaligenes eutrophus H16. II. The isolation and characterization of mutants auxotrophic for phenylalanine and tyrosine. Arch Microbiol. 1975 Apr 7;103(2):141–149. doi: 10.1007/BF00436341. [DOI] [PubMed] [Google Scholar]
  7. Friedrich C. G. Depression of hydrogenase during limitation of electron donors and derepression of ribulosebisphosphate carboxylase during carbon limitation of Alcaligenes eutrophus. J Bacteriol. 1982 Jan;149(1):203–210. doi: 10.1128/jb.149.1.203-210.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Friedrich C. G., Friedrich B. Regulation of hydrogenase formation is temperature sensitive and plasmid coded in Alcaligenes eutrophus. J Bacteriol. 1983 Jan;153(1):176–181. doi: 10.1128/jb.153.1.176-181.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  10. Merberg D., O'Hara E. B., Maier R. J. Regulation of hydrogenase in Rhizobium japonicum: analysis of mutants altered in regulation by carbon substrates and oxygen. J Bacteriol. 1983 Dec;156(3):1236–1242. doi: 10.1128/jb.156.3.1236-1242.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Repaske R., Repaske A. C. Quantitative requirements for exponential growth of Alcaligenes eutrophus. Appl Environ Microbiol. 1976 Oct;32(4):585–591. doi: 10.1128/aem.32.4.585-591.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schink B., Schlegel H. G. Mutants of Alcaligenes eutrophus defective in autotrophic metabolism. Arch Microbiol. 1978 May 30;117(2):123–129. doi: 10.1007/BF00402299. [DOI] [PubMed] [Google Scholar]
  13. Schink B., Schlegel H. G. The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties. Biochim Biophys Acta. 1979 Apr 12;567(2):315–324. doi: 10.1016/0005-2744(79)90117-7. [DOI] [PubMed] [Google Scholar]
  14. Schneider K., Cammack R., Schlegel H. G., Hall D. O. The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus. Biochim Biophys Acta. 1979 Jun 19;578(2):445–461. doi: 10.1016/0005-2795(79)90175-2. [DOI] [PubMed] [Google Scholar]
  15. Schneider K., Schlegel H. G. Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16. Biochem J. 1981 Jan 1;193(1):99–107. doi: 10.1042/bj1930099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schneider K., Schlegel H. G. Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16. Biochim Biophys Acta. 1976 Nov 8;452(1):66–80. doi: 10.1016/0005-2744(76)90058-9. [DOI] [PubMed] [Google Scholar]
  17. Wilde E., Schlegel H. G. Oxygen tolerance of strictly aerobic hydrogen-oxidizing bacteria. Antonie Van Leeuwenhoek. 1982 May;48(2):131–143. doi: 10.1007/BF00405198. [DOI] [PubMed] [Google Scholar]

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