1995
DOI: 10.1002/9780470123171.ch3
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Cytochrome c Oxidase: Chemistry of a Molecular Machine

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Cited by 10 publications
(11 citation statements)
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“…It translocates protons across the inner membrane of mitochondria by utilizing the chemical energy harnessed from the four-electron reduction reaction of dioxygen to water. 13 The oxygen reduction chemistry takes place in a binuclear center, comprised of a high-spin heme group (heme a 3 ) and a Cu B center ~5 Å from the heme iron atom (Figure 1). 4,5 The presence of the Cu B in the binuclear center introduces an intriguing twist to the ligand binding properties of the heme iron as compared to other hemeproteins, due to the high affinity of Cu B toward diatomic heme iron ligands.…”
mentioning
confidence: 99%
“…It translocates protons across the inner membrane of mitochondria by utilizing the chemical energy harnessed from the four-electron reduction reaction of dioxygen to water. 13 The oxygen reduction chemistry takes place in a binuclear center, comprised of a high-spin heme group (heme a 3 ) and a Cu B center ~5 Å from the heme iron atom (Figure 1). 4,5 The presence of the Cu B in the binuclear center introduces an intriguing twist to the ligand binding properties of the heme iron as compared to other hemeproteins, due to the high affinity of Cu B toward diatomic heme iron ligands.…”
mentioning
confidence: 99%
“…The Cu A site, which consists of a Cu(I)Cu(II) bridged by two thiolates, is electron rich and is poised to act as a conformational trigger upon reduction by an additional electron (67). We expect conformational changes at the dioxygen reduction site as well in order to optimize the biological energy transduction (Figure 2) …”
Section: Wwwannualreviewsorg • Adventures With Molecular Machinesmentioning
confidence: 99%
“…Redox-linked proton pumping in CcO is a highly complex process consisting of electron input, electron transfer, proton uptake, redox linkage, and proton ejection steps (86). However, without redox linkage there can be no transfer of redox energy from the electron degrees of freedom to the protein degrees of freedom, and therefore no proton pumping (66,67). The putative redox linkage could occur only during the second half of the turnover cycle when the final two electrons are passed to the activated dioxygen, i.e., when the peroxide and the oxyferryl intermediates are presumably formed (67).…”
Section: Wwwannualreviewsorg • Adventures With Molecular Machinesmentioning
confidence: 99%
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