Bio-inorganic Lab
Heme-copper oxidases (HCOs) are a superfamily of terminal oxidases in the respiratory chains of both eukaryotic mitochondria and bacteria. They all contain a heteronuclear heme-copper center where O2 binding, activation, and reduction to water occur. The heme-copper center is unique in that it contains not only a heme with a proximal histidine ligand, commonly found in other heme proteins, such as Mb and HO, but also a copper center (called CuB) that is coordinated to three histidines and is within ≈5 â„« of the heme iron center. Understanding the structure and function of this heme-copper center has been the focus of intense biochemical, spectroscopic, x-ray crystallographic, and biomimetic modeling studies.
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Proc. Natl. Acad. Sci. U. S. A. 2002, 100, 3629−3634.
Cytochrome P450 (CYP, P450) enzymes constitute one of the largest gene superfamilies found in nature. P450s occur in the Bacteria, Archaea, and the Eukarya; they have also been discovered in some viruses. P450s have extremely diverse functions, playing essential roles in the metabolism of endogenous and exogenous molecules—ranging from the biosynthesis and degradation of sterols, vitamins, and various secondary metabolites to the detoxification and activations of drugs and pollutants. At the molecular level, P450s are b-type heme-thiolate proteins that generally catalyze the molecular scission of atmospheric dioxygen, inserting one oxygen atom into the substrate whilst the second oxygen atom is reduced to a single water molecule.
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Sci. Rep. 2022, 12, 16232-16246
