Catalytic cycle of cytochrome-c3 hydrogenase, a [NiFe]-enzyme, deduced from the structures of the enzyme and the enzyme mimic

Tatsuhiko Yagi, Seiji Ogo, Yoshiki Higuchi

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    7 Citations (Scopus)


    Hydrogenases catalyze uptake and production of H2. Heterolytic cleavage of H2 bound on [NiFe]-hydrogenase (E) produces two unequal H species to form E:HaHb, where Ha and Hb behave differently. The structures of various states of the enzyme established by crystallography and spectroscopy were used to construct a catalytic cycle of the enzyme. The Ni-Fe center of the active enzyme has the Ni-Fe bridging site vacant. The enzyme is suggested to bind H2 either at Ni or Fe atom. In E:HaHb, Ha is considered to be a protein-bound hydron (proton or deuteron) at the entrance to the hydrophobic gas tunnel. The structure of a synthetic hydrogenase-mimic suggests Hb to be the 6th ligand to Fe. Two successive one-electron processes from E:HaHb complete the catalytic cycle of H2 uptake. The reverse of the cycle operates in the H2 production. The proposed catalytic cycle is consistent with the kinetic, crystallographic and spectroscopic studies.

    Original languageEnglish
    Pages (from-to)18543-18550
    Number of pages8
    JournalInternational Journal of Hydrogen Energy
    Issue number32
    Publication statusPublished - Oct 31 2014

    All Science Journal Classification (ASJC) codes

    • Renewable Energy, Sustainability and the Environment
    • Fuel Technology
    • Condensed Matter Physics
    • Energy Engineering and Power Technology


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