Abstract
This review focuses on the type A cytochrome c oxidases (CcO), which are found in all mitochondria and also in several aerobic bacteria. CcO 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 CcO 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 CcO, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 2469-2490 |
| Number of pages | 22 |
| Journal | Chemical Reviews |
| Volume | 118 |
| Issue number | 5 |
| Early online date | 19 Jan 2018 |
| DOIs | |
| Publication status | Published - 14 Mar 2018 |
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Oxygen Activation and Energy Conservation by Cytochrome c Oxidase. / Wikström, Mårten; Krab, Klaas; Sharma, Vivek.
In: Chemical Reviews, Vol. 118, No. 5, 14.03.2018, p. 2469-2490.Research output: Contribution to Journal › Review article › Academic › peer-review
TY - JOUR
T1 - Oxygen Activation and Energy Conservation by Cytochrome c Oxidase
AU - Wikström, Mårten
AU - Krab, Klaas
AU - Sharma, Vivek
PY - 2018/3/14
Y1 - 2018/3/14
N2 - This review focuses on the type A cytochrome c oxidases (CcO), which are found in all mitochondria and also in several aerobic bacteria. CcO 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 CcO 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 CcO, 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.
AB - This review focuses on the type A cytochrome c oxidases (CcO), which are found in all mitochondria and also in several aerobic bacteria. CcO 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 CcO 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 CcO, 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=85043781627&partnerID=8YFLogxK
U2 - 10.1021/acs.chemrev.7b00664
DO - 10.1021/acs.chemrev.7b00664
M3 - Review article
VL - 118
SP - 2469
EP - 2490
JO - Chemical Reviews
JF - Chemical Reviews
SN - 0009-2665
IS - 5
ER -