Redox-Bohr effect in electron/proton energy transduction: Cytochrome c3 coupled to hydrogenase works as a 'proton thruster' in Desulfovibrio vulgaris

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Abstract

A central step in the metabolism of Desulfovibrio spp. is the oxidation of molecular hydrogen catalyzed by a periplasmic hydrogenase. However, this enzymatic activity is quite low at physiological pH. The hypothesis that, in the presence of the tetrahaem cytochrome c3, hydrogenase can maintain full activity at physiological pH through the concerted capture of the resulting electrons and protons by the cytochrome was tested for the case of Desulfovibrio vulgaris (Hildenborough). The crucial step involves an electron-to-proton energy transduction, and is achieved through a net-work of cooperativities between redox and ionizable centers within the cytochrome (redox-Bohr effect). This mechanism, which requires a relocation of the proposed proton channel in the hydrogenase structure, is similar to that proposed for the transmembrane proton pumps, and is the first example which shows evidence of functional energy transduction in the absence of a membrane confinement.

Original languageEnglish
Pages (from-to)488-491
Number of pages4
JournalJournal of Biological Inorganic Chemistry
Volume2
Issue number4
DOIs
Publication statusPublished - 1 Aug 1997

Keywords

  • Cytochrome c
  • Electron transfer
  • Energy transduction
  • Proton transfer
  • Redox-Bohr

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