Oxygen Activation and Energy Conservation by Cytochrome c Oxidase

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Wikström , M K F , Krab , K & Sharma , V 2018 , ' Oxygen Activation and Energy Conservation by Cytochrome c Oxidase ' , Chemical Reviews , vol. 118 , no. 5 , pp. 2469–2490 . https://doi.org/10.1021/acs.chemrev.7b00664

Title: Oxygen Activation and Energy Conservation by Cytochrome c Oxidase
Author: Wikström, Mårten Karl Fredrik; Krab, Klaas; Sharma, Vivek
Contributor organization: Institute of Biotechnology
Department of Physics
Date: 2018-03-14
Language: eng
Number of pages: 22
Belongs to series: Chemical Reviews
ISSN: 0009-2665
DOI: https://doi.org/10.1021/acs.chemrev.7b00664
URI: http://hdl.handle.net/10138/256025
Abstract: This review focuses on the type A cytochrome c oxidases (C cO), which are found in all mitochondria and also in several aerobic bacteria. C cO catalyzes the respiratory reduction of dioxygen (O2) to water by an intriguing mechanism, the details of which are fairly well understood today as a result of research for over four decades. Perhaps even more intriguingly, the membrane-bound C cO couples the O2 reduction chemistry to translocation of protons across the membrane, thus contributing to generation of the electrochemical proton gradient that is used to drive the synthesis of ATP as catalyzed by the rotary ATP synthase in the same membrane. After reviewing the structure of the core subunits of C cO, the active site, and the transfer paths of electrons, protons, oxygen, and water, we describe the states of the catalytic cycle and point out the few remaining uncertainties. Finally, we discuss the mechanism of proton translocation and the controversies in that area that still prevail.
Subject: 116 Chemical sciences
114 Physical sciences
HEME-COPPER OXIDASES
PROTON-PUMPING MECHANISM
COUPLED ELECTRON-TRANSFER
O BOND-CLEAVAGE
ZETA VALENCE QUALITY
ACTIVE-SITE TYROSINE
GAUSSIAN-BASIS SETS
X-RAY-STRUCTURE
LOW-SPIN HEME
RHODOBACTER-SPHAEROIDES
Peer reviewed: Yes
Rights: unspecified
Usage restriction: openAccess
Self-archived version: publishedVersion


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