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Hydrogenase of purple bacteria: properties and regulation of synthesis

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Physico-chemical properties of homogeneous preparations of soluble and membrane-bound hydrogenases from the purple sulfur bacterium Thiocapsa roseopersicina BBS and membrane-bound hydrogenase of Rhodopseudomonas capsulata, strain B10 have been studied. Compared to the enzymes from other sources, the hydrogenase of Thiocapsa roseopersicina is more stable to O2 and products of its reduction (O 2 - , H2O2), temperature and a number of other factors of the medium. A natural electron donor for T. roseopersicina hydrogenase is a low-potential cytochrome C′3, while the natural electron acceptors for hydrogenases of R. capsulata, T. roseopersicina, Ectothiorhodospira shaposhnikovii and Anabaena cylindrica are cytochromes of groups “c” and “b”.

In different phototrophs, synthesis of hydrogenase can be inhibited by the presence of high concentrations of O2. In some microorganisms (e.g. Rhodopseudomonas capsulata, strain B10) the repressing effect on hydrogenase formation is also exhibited by organic compounds. H2 may not necessarily be present for hydrogenase synthesis by purple bacteria, but its presence may considerable increase the level of the enzyme.

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sodium dodecylsulfate


high-potential iron — sulfur protein

R :


T :


Rh :


C :



  1. Adams MWW, Mortenson LE, Chen J-S (1980) Hydrogenase. Biochim Biophys Acta 594:105–176

  2. Albracht SPJ, Graf E-G, Thauer RK (1982) The EPR properties of nickel in hydrogenase from Methanobacterium thermoautotrophicum. FEBS Lett 140:311–313

  3. Arp DJ, Burris RH (1979) Purification and properties of the particulate hydrogenase from the bacteriodes soybean root nodules. Biochim Biophys Acta 570:221–230

  4. Berlier YM, Lespinat PA (1980) Mass-spectrometrical kinetic studies of the nitrogenase and hydrogenase activities in vivo cultures of Azospirillum brasilense. Arch Microbiol 125:67–72

  5. Bowien B, Schlegel HG (1981) Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria. Annu Rev Microbiol 35:405–452

  6. Cammack R, Patil D, Aquirre R, Hatchkian EE (1982) Redox properties of the ESR-detectable nickel in hydrogenase from Desulfovibrio gigas. FEBS Lett 142:289–292

  7. Chen J-S (1978) Structure and function of two hydrogenase from dinitrogen-fixing bacterium Clostridium pasteurianum. In: Schlegel HG, Schneider K (eds) Hydrogenases: Their Catalytic Activity, Structure and Function, Goltze E, Göttingen, pp 57–81

  8. Colbeau A, Vignais PM (1981) The membrane-bound hydrogenase of Rh. capsulata: stability and catalytic properties. Biochim Biophys Acta 662:271–284

  9. Colbeau A, Chabert F, Vignais PM (1978) Hydrogenase activity in Rhodopseudomonas capsulata. Stability and stabilization of the solubilized enzyme. In: Schlegel HG, Schneider K (eds) Hydrogenases: Their Catalytic Activity, Structure and Function, Goltze E, Göttingen, pp 183–198

  10. Friedrich CG (1982) Derepression of hydrogenase during limitation of electron donors and derepression of ribulose-bisphosphate carboxylase during carbon limitation of Alcaligenes eutrophus. J Bacteriol 152:42–48

  11. Friedrich CG, Schneider K, Friedrich B (1982) Nickel in the catalytically active hydrogenase of Alcaligenes eutrophus. J Bacteriol 152:42–48

  12. Fuchs G, Moll J, Scherer P, Thauer R (1978) Activity, acceptor specificity and function of hydrogenase in Methanobacterium thermoautotrophicum. In: Schlegel HG, Schneider K (eds) Hydrogenases: Their Catalytic Activity, Structure and Function. Goltze, Göttingen, pp 83–92

  13. Gitlitz PH, Krasna AJ (1975) Structural and catalytical properties of hydrogenase from Chromatium. Biochemistry 14:2561–2567

  14. Gogotov IN (1973) Hydrogen metabolism and nitrogen fixation in phototrophic bacteria. In: Abstracts of Symp. on Procaryotic Photosyn. Organisms, Freiburg, pp 118–131

  15. Gogotov IN (1978) Relationships in hydrogen metabolism between hydrogenase and nitrogenase in phototrophic bacteria. Biochimie 60:267–275

  16. Gogotov IN (1979) Hydrogenases of microorganisms. Uspekhi mikrobiologii 14:3–27

  17. Gogotov IN (1980) Microorganisms as hydrogen and hydrogenase producers. In: Wingard LB, Berezin IV (eds) Enzyme Enginering: Future Directions, Plenum Press, NY-L-W, pp 321–337

  18. Gogotov IN (1984) Hydrogen production by gron cultures, cell suspension and polyenzyme systems of phototrophic bacteria. In: Berezin IV et al. (eds) Solar Energy Bioconversion. Pushchino, pp 75–85

  19. Gogotov IN, Zorin NA, Bogorov LV (1974) Metabolism of hydrogen and nitrogen fixation capacity of Thiocapsa roseopersicina Mikrobiologiya 43:5–10

  20. Gogotov IN, Zorin NA, Serebriakova LT, Kondratieva EN (1978) The properties of hydrogenase from Thiocapsa roseopersicina Biochim Biophys Acta 523:385–393

  21. Hatchikian EC, Bruschi M, Le Gall J (1978) Characterization on the periplasmic hydrogenase from Desulfovibrio gigas. Biochem Biophys Res Communs 82:451–461

  22. Klemme L-H (1968) Untersuchungen zur Photoautotrophic mit Molekularen Wasserstoff bei neuisolierten schwefelfreien Purpurbakterien. Arch Mikrobiol 64:29–42

  23. Kondratieva EN, Gogotov IN (1981) Molecular hydrogen in the metabolism of microorganisms. Moscow, Nauka, pp 342

  24. Kondratieva EN, Gogotov IN (1983) Production of molecular hydrogen in microorganisms. In: Adv Biochem Eng Fiechter A (ed), Springer, v. 28, B.-H.-N.Y., pp 139–191

  25. Korsunsky OF, Smolygina LD, Laurinavichene TV, Gogotov IN (1982) Properties and functions of low-potential cytochrome c3 from Thiocapsa roseopersicina. Biokhimiya 47:355–360

  26. Krasna AI (1980) Regulation of hydrogenase activity in Enterobacteria. J Bacteriol 144:1094–1097

  27. Kulakova SM, Yakunin AF, Gogotov IN (1982) Stability of purple bacteria hydrogenase and nitrogenase to the inactivating action of oxygen and the products of its reduction. Prikl biokhim i mikrobiol 18:324–330

  28. Maier RJ, Hanus FJ, Evans HJ (1979) Rgulation of hydrogenase in Rhizobium japonicum. J Bacteriol 137:824–829

  29. Meyer J, Kelley BC, Vignais PM (1978) Nitrogen fixation and hydrogen metabolism in photosynthetic bacteria. Biochimie 60:245–260

  30. Mortenson LE, Chen J-S (1974) Hydrogenase. In: Heiland JB (ed) Microbiol Iron Metabolism. Acad Press, New York, pp 231–282

  31. Partridge CDP, Walker CC, Yates MG, Postgate JR (1980) The relationship between hydrogenase and nitrogenase in Azotobacter chroococcum: effect of N-source on hydrogenase activity. J Gen Microbiol 119:313–319

  32. Quist RC, Stokes JL (1972) Comparative effect of temperature on the induced synthesis of hydrogenase and enzymes of the benzoate oxidation system in psychrophilic and mesophilic bacteria. Can J Microbiol 18:1233–1239

  33. Schlegel HG, Eberhardt U (1972) Regulatory phenomena in the metabolism of knallgasbacteria. Adv Microbiol Physiol 7:205–243

  34. Strekas T, Antanaitis BC, Krasna AJ (1980) Characterization and stability of hydrogenase from Chromatium. Biochim Biophys Acta 116:1–9

  35. Tsygankov AA, Gogotov IN (1979) Continuous cultivation of phototrophic bacteria. Prikl biokhim i mikrobiol 5:665–670

  36. Tsygankov AA, Yakunin AF, Gogotov IN (1982a) Hydrogenase activity of Rhodopseudomonas capsulata during growth on organic media. Mikrobiologiya 51:533–537

  37. Tsygankov AA, Pavlova EA, Gogotov IN (1982b) Activity of some enzymes involved in H2 metabolism of Rhodopseudomonas capsulata depending on growth conditions of the cultures. Mikrobiologiya 51:188–193

  38. Van der Werf A, Yates MG (1978) Hydrogenase from nitrogenfixing Azotobacter chroococcum. In: Schlegel HG, Schneider K (eds) Hydrogenases: Their Catalytic Activity, Structure and Function. Goltze, Göttingen, pp 307–326

  39. Yagi T, Endo A, Tsuji K (1978) Properties of hydrogenase from particulate fraction of Desulfovibrio vulgaris. In: Schlegel HG, Schneider K (eds) Hydrogenases: Their Catalytic Activity, Structure and Function. Goltze, Göttingen, pp 107–124

  40. Zorin NA, Gogotov IN (1980) Purification and properties of cytochrome c552 from purple sulfur bacterium Thiocapsa roseopersicina. Biokhimiya 45:1497–1502

  41. Zorin NA, Gogotov IN (1982) Stability of hydrogenase of purple sulfur bacterium Thiocapsa roseopersicina. Biokhimiya 47:827–833

  42. Zorin NA, Gogotov IN (1983) High-potential iron-sulfur protein of Thiocapsa roseopersicina. Biokhimiya 48:1181–1187

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This paper is dedicated to Professor Dr. H.G. Schlegel in honour of his sixtieth birthday and in recognition of his great contribution in the field of physiology and biochemistry of microorganisms capable of using H2. Professor H.G. Schlegel had a profound and most fuitful influence on the progress in the research of the laboratory headed by the author

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Gogotov, I.N. Hydrogenase of purple bacteria: properties and regulation of synthesis. Arch. Microbiol. 140, 86–90 (1984). https://doi.org/10.1007/BF00409777

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Key words

  • H2 metabolism
  • Hydrogenase regulation
  • Hydrogenase properties
  • Purple bacteria