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Cytochromeb 50 as a proton carrier in the photosynthetic redox chain of purple bacteria

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Abstract

Recent data on the proton-translocating activity ofb cytochromes in chromatophores of purple bacteria and their arrangement in the photosynthetic redox chain are discussed. These data appear to support the concept of theb 50 andb −90 cytochrome doublet spanning the membrane. Current schemes of H+ transport byb cytochromes are considered, and the scheme of H+ translocation by cytochromeb 50 taking up H+ at the outer side of the membrane and a quinone delivering them from this cytochrome to the inner space of the chromatophore is favored as the most probable in the light of recent findings. This scheme is applicable both to Crofts' linear model of the redox chain and to Mitchell's Q cycle. Kinetic discrepancies between H+ uptake and cytochromeb 50 reduction at high ambient redox potentials are interpreted in terms of a special, cytochromeb 50-independent, yet Rieske FeS-protein-dependent mode of H+ transport.

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Authors and Affiliations

  1. Department of Microbiology, Moscow State University, 117234, Moscow, USSR

    Alexander V. Oleskin & Vitaly D. Samuilov

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  1. Alexander V. Oleskin
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  2. Vitaly D. Samuilov
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Oleskin, A.V., Samuilov, V.D. Cytochromeb 50 as a proton carrier in the photosynthetic redox chain of purple bacteria. J Bioenerg Biomembr 15, 167–177 (1983). https://doi.org/10.1007/BF00743938

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  • DOI: https://doi.org/10.1007/BF00743938

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