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| − | Please input one-sentence summary here.
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| − | ==Annotated Information==
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| − | ===Function===
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| − | Cytochrome c oxidase subunit I (CO1 or MT-CO1) is one of three mitochondrial DNA (mtDNA) encoded subunits (MT-CO1, MT-CO2, MT-CO3) of respiratory complex IV. Complex IV is the third and final enzyme of the electron transport chain of mitochondrial oxidative phosphorylation.
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| − | Cytochrome c oxidase is a key enzyme in aerobic metabolism. Proton pumping heme-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-heme a3 (or heme o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases, is directly involved in the coupling between dioxygen reduction and proton pumping.Some terminal oxidases generate a transmembrane proton gradient across the mitochondrial inner membrane.
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| − | The enzyme complex consists of 3-4 subunits up to 13 polypeptides in different species of which only the catalytic subunit I (COI)) is found in all heme-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin heme and copper B) as well as a low-spin heme, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within COI is common to all family members. The enzyme complexes vary in heme and copper composition, substrate type and substrate affinity. The different respiratory oxidases allow the cells to customize their respiratory systems according to a variety of environmental growth conditions.
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| − | ===Expression===
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| − | Please input expression information here.
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| − | ===Evolution===
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| − | It has been suggested that cytochrome c oxidase catalytic subunits evolved from ancient nitric oxide reductases that could reduce both nitrogen and oxygen. MT-CO1 sequence differences are too small to be detected between closely related species, more than 2% sequence divergence has been detected between such organisms. In most seed plants, the rate of evolution of cox1 is very slow.
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| − | ===Inhibitor===
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| − | Cyanide, sulfide, azide, and carbon monoxide they all can inhibite the function of cytochrome c oxidas.
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| − | ==Labs working on this gene==
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| − | Please input related labs here.
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| − | ==References==
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| − | Kosakyan A, Heger TJ, Leander BS, Todorov M, Mitchell EA, Lara E (May 2012). "COI barcoding of Nebelid testate amoebae (Amoebozoa: Arcellinida): extensive cryptic diversity and redefinition of the Hyalospheniidae Schultze". Protist 163 (3): 415–34.doi:10.1016/j.protis.2011.10.003
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| − | Saraste M, Castresana J, Higgins DG, Lubben M (1994). "Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen". EMBO J. 13 (11): 2516–2525
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| − | Capaldi RA, Malatesta F, Darley-Usmar VM (1983). "Structure of cytochrome c oxidase". Biochim. Biophys. Acta 726 (2): 135–48. doi:10.1016/0304-4173(83)90003-4
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| − | ==Structured Information==
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