Cytochrome Oxidase at the Membrane/Water Interface : Mechanism of Functioning and Molecular Recognition

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A concerted 2:1:1-electron mechanism for cytochrome oxidase functioning is evaluated by thermodynamic and kinetic analysis. Possible ways of dioxygen reduction to water as well as the stoichiometry of the proton pump are analyzed thermodynamically. The conditions are formulated for the occurrence of multielectron oxygen reduction. Kharkats and Volkov first presented proofs that cytochrome c oxidase reduces molecular oxygen by synchronous multielectron mechanism without O2- intermediate formation (Yu. I. Kharkats and A. G. Volkov, Biochim. Biophys. Acta, 891, 56 (1987)). As the field progresses after this pioneering observations, it became clear that the first step of dioxygen reduction is two-electron concerted process. As follows from thermodynamics energy for the H+-pump functioning is liberated only at the last two steps of water formation on addition of third and fourth electrons independently of the reaction pathway. The media reorganization energy corresponding to simultaneous electrons and protons transfer will be minimal in the case then the directions of their transfers are close. In mitochondrial cytochrome c oxidase the donor of electrons is placed on the side C and the protons comes from the side M. In this case the minimal activation energy will be achieved at maximal possible at given geometry of the system angle between the directions of electrons and protons transfer.

収録刊行物

  • Analytical sciences : the international journal of the Japan Society for Analytical Chemistry  

    Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 14(1), 27-30, 1998-02-10 

    社団法人 日本分析化学会

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各種コード

  • NII論文ID(NAID)
    10002413856
  • NII書誌ID(NCID)
    AA10500785
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09106340
  • NDL 記事登録ID
    4406418
  • NDL 雑誌分類
    ZP4(科学技術--化学・化学工業--分析化学)
  • NDL 請求記号
    Z54-F482
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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