IMR Press / FBL / Volume 18 / Issue 1 / DOI: 10.2741/4086

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Review

Steps of the coupled charge translocation in the catalytic cycle of cytochrome c oxidase

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1 A.N.Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia
Front. Biosci. (Landmark Ed) 2013, 18(1), 36–57; https://doi.org/10.2741/4086
Published: 1 January 2013
Abstract

Cytochrome c oxidase (COX) terminates the respiratory chain in mitochondria and in plasmatic membrane of many aerobic bacteria. The enzyme reduces dioxygen molecule into water and the reaction is accompanied with generation of transmembrane difference of electric potentials. The energy conservation by COX is based on the vectorial organization of the chemical reaction due to substrate protons transfer from the negative phase into the active site to meet the electrons, coming from opposite side of the membrane. In addition, a half of free energy of redox-chemistry reaction is conserved through transmembrane proton pumping. Each of the reaction steps in the catalytic cycle of COX involves a sequence of coupled electron and proton transfer reaction. The timeresolved study of the coupled charge translocation during catalytic cycle of cytochrome c oxidase is reviewed. Based on many fascinating parallels between the mechanisms of COX and pigment-protein complex of photosystem II from oxygenic photosynthetic organisms, the data described could be used in the light-driven water-splitting process.

Keywords
Cytochrome
Oxidase
Protons
Membrane potential
Channels
Electrogenic
Voltage
Electron injection
Review
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