期刊
FEBS LETTERS
卷 566, 期 1-3, 页码 126-130出版社
WILEY
DOI: 10.1016/j.febslet.2004.04.016
关键词
cytochrome c oxidase; proton pumping; coupled electron-proton transfer; catalytic cycle
资金
- NIGMS NIH HHS [GM54052] Funding Source: Medline
Using electrostatic calculations, we have examined the dependence of the protonation state of cytochrome c oxidase from bovine heart on its redox state. Based on these calculations, we propose a possible scheme of redox-finked proton pumping. The scheme involves His291 - one of the ligands of the Cu-B redox center - which plays the role of the proton loading site (PLS) of the pump. The mechanism of pumping is based on ET reaction between two hemes of the enzyme, which is coupled to a transfer of two protons. Upon ET, the first proton (fast reaction) is transferred to the PLS (His291), while subsequent transfer of the second chemical proton to the binuclear center (slow reaction) is accompanied by the ejection of the first (pumped) proton. Within the proposed model, we discuss the catalytic cycle of the enzyme. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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