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Hydrogenase of purple bacteria: properties and regulation of synthesis

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Abstract

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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Abbreviations

SDS:

sodium dodecylsulfate

Hipip:

high-potential iron — sulfur protein

R :

Rhodopseudomonas

T :

Thiocapsa

Rh :

Rhodospirillum

C :

Chromatium

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Authors and Affiliations

  1. Institute of Soil Science and Photosynthesis, USSR Academy of Sciences, 142292, Pushchino, USSR

    Ivan N. Gogotov

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  1. Ivan N. Gogotov
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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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  • DOI: https://doi.org/10.1007/BF00409777

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