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- W2476367058 abstract "The heme-copper oxidases (historically termed cytochrome oxidases) are ubiquitous in both prokaryotic and eukaryotic aerobic organisms. They function to catalyze the 4-proton, 4-electron reduction of dioxygen to water and transduce the energy made available from O-O bond cleavage to the translocation of an additional 4 protons across the cytoplasmic or mitochondrial membrane. The energy released is stored as an electrochemical gradient and utilized to drive ATP synthesis in the process known as oxidative phosphorylation. For these reasons, heme-copper oxidases are arguably the most important enzymes in mammalian cells, providing the energy for most metabolic processes and consuming 80-90% of the oxygen we breathe. The catalytic activity of the heme copper oxidases resides in subunit I which is a membrane-spanning polypeptide, containing a dinuclear high-spin heme-CuB dioxygen binding site and a low-spin heme center. A second subunit (II) contains the binding site for the electron donor. A number of differing classes" @default.
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- W2476367058 date "1998-06-09" @default.
- W2476367058 modified "2023-10-16" @default.
- W2476367058 title "XAS Studies on the Cu<sub>A</sub> Centers of Heme-Copper Oxidases and Loop-Directed Mutants of Azurin: Implications for Redox Reactivity" @default.
- W2476367058 doi "https://doi.org/10.1021/bk-1998-0692.ch013" @default.
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