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| | ==Annotated Information== | | ==Annotated Information== |
| | ===Function=== | | ===Function=== |
| − | 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=== | | ===Expression=== |
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| | ===Evolution=== | | ===Evolution=== |
| − | 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== | | ==Labs working on this gene== |
| − | the Institute for Protein Research, Osaka University, Yamada-oka, Suita , Japan.
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| − | European Molecular Biology Laboratory, Meyerhofstrasse ,Heidelberg, Germany.
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| | ==References== | | ==References== |
| − | Tsukihara T, Aoyama H, Yamashita E, et al.(1996).The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science 272
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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.
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| − | Capaldi RA, Malatesta F, Darley-Usmar VM.(1983).Structure of cytochrome c oxidase". Biochim. Biophys. Acta.
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| − | Hebert PD, Ratnasingham S, deWaard JR.(2003).Barcoding animal life: cytochrome c oxidase subunit 1 divergences among closely related species. Proc. Biol. Sci.
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| | ==Structured Information== | | ==Structured Information== |
Please input one-sentence summary here.
Annotated Information
Function
Please input function information here.
Expression
Please input expression information here.
Evolution
Please input evolution information here.
You can also add sub-section(s) at will.
Labs working on this gene
Please input related labs here.
References
Please input cited references here.
Structured Information
| Gene Name
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{{{GeneName}}}
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| Description
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{{{Description}}}
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| Version
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{{{Version}}}
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| Length
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{{{Length}}}
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| Definition
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{{{Definition}}}
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| Source
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{{{Source}}}
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| Chromosome
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{{{Chromosome}}}
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| Location
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{{{AP}}}
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| Sequence Coding Region
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{{{CDS}}}
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| Genome Context
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{{{GCID}}}
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Gene Structure
(RNA Editing)
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{{{GSID}}}
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| Protein Sequence
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{{{AA}}}
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| Gene Sequence
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{{{DNA}}}
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| External Link(s)
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{{{Link}}}
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