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• W137446206 startingPage "89" @default.
• W137446206 abstract "Cytochrome c oxidase (CcO) is the terminal oxidase of cell respiration which reduces molecular oxygen (O2) to H2O coupled with the proton pump. For elucidation of the mechanism of CcO, the three-dimensional location and chemical reactivity of each atom composing the functional sites have been extensively studied by various techniques, such as crystallography, vibrational and time-resolved electronic spectroscopy, since the X-ray structures (2.8 Å resolution) of bovine and bacterial CcO have been published in 1995. X-ray structures of bovine CcO in different oxidation and ligand binding states showed that the O2 reduction site, which is composed of Fe (heme a 3) and Cu (CuB), drives a non-sequential four-electron transfer for reduction of O2 to water without releasing any reactive oxygen species. These data provide the crucial structural basis to solve a long-standing problem, the mechanism of the O2 reduction. Time-resolved resonance Raman and charge translocation analyses revealed the mechanism for coupling between O2 reduction and the proton pump: O2 is received by the O2 reduction site where both metals are in the reduced state (R-intermediate), giving the O2-bound form (A-intermediate). This is spontaneously converted to the P-intermediate, with the bound O2 fully reduced to 2 O2−. Hereafter the P-intermediate receives four electron equivalents from the second Fe site (heme a), one at a time, to form the three intermediates, F, O, and E to regenerate the R-intermediate. Each electron transfer step from heme a to the O2 reduction site is coupled with the proton pump. X-ray structural and mutational analyses of bovine CcO show three possible proton transfer pathways which can transfer pump protons (H) and chemical (water-forming) protons (K and D). The structure of the H-pathway of bovine CcO indicates that the driving force of the proton pump is the electrostatic repulsion between the protons on the H-pathway and positive charges of heme a, created upon oxidation to donate electrons to the O2 reduction site. On the other hand, mutational and time-resolved electrometric findings for the bacterial CcO strongly suggest that the D-pathway transfers both pump and chemical protons. However, the structure for the proton-gating system in the D-pathway has not been experimentally identified. The structural and functional diversities in CcO from various species suggest a basic proton pumping mechanism in which heme a pumps protons while heme a 3 reduces O2 as proposed in 1978." @default.
• W137446206 created "2016-06-24" @default.
• W137446206 creator A5028432382 @default.
• W137446206 creator A5061670036 @default.
• W137446206 creator A5071154631 @default.
• W137446206 date "2014-12-01" @default.
• W137446206 modified "2023-10-12" @default.
• W137446206 title "Respiratory Conservation of Energy with Dioxygen: Cytochrome c Oxidase" @default.
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• W137446206 doi "https://doi.org/10.1007/978-3-319-12415-5_4" @default.
• W137446206 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25707467" @default.
• W137446206 hasPublicationYear "2014" @default.
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