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• W4254334879 abstract "Abstract Cytochrome c oxidase reduces molecular oxygen (O 2 ) to water (coupled with proton pumping) at its O 2 reduction site composed of an iron ion (heme a 3 ) and a copper ion (Cu B ) by electrons transferred from cytochrome c in the intermembrane space by Cu A and heme a in the enzyme protein and by protons from the matrix space. Mitochondrial cytochrome c oxidase, isolated from bovine heart muscle as early as in 1941, was crystallized to determine the X‐ray structure at 2.3/2.35 Å resolutions in the fully oxidized/reduced states in 1998, showing 13 different subunits and Cu B , liganded with three histidine imidazole groups in a trigonal‐planer coordination in the fully reduced state. A tyrosine phenol group is fixed close to the O 2 reduction site with a covalent link with one of the three imidazole groups. This O 2 reduction site structure suggests that Fe a 3 O 2 and Fe a 3 OOH are stable and unstable, respectively, to form FeO as the second intermediate in the O 2 reduction process, consistent with the resonance Raman results for the process. A fairly big redox‐coupled X‐ray structural change in an aspartate (Asp51) located near the intermembrane surface of the enzyme molecule suggesting a large redox‐coupled pKa change in Asp51 and a hydrogen bond network connecting Asp51 with the matrix surface indicate that Asp51 is the site for proton pumping. A peptide bond in the hydrogen bond network facilitates the unidirectional proton transfer through the hydrogen bond network up to Asp51." @default.
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• W4254334879 date "2004-03-05" @default.
• W4254334879 modified "2023-09-26" @default.
• W4254334879 title "Mitochondrial Cytochrome <i> <scp>c</scp> </i> Oxidase" @default.
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• W4254334879 doi "https://doi.org/10.1002/0470028637.met126" @default.
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