Cytochrome c oxidase subunit I

451217708ENSG00000198804ENSMUSG00000064351P00395P00397n/an/an/aNP_904330Cytochrome c oxidase I (COX1) also known as mitochondrially encoded cytochrome c oxidase I (MT-CO1) is a protein that in humans is encoded by the MT-CO1 gene. In other eukaryotes, the gene is called COX1, CO1, or COI. Cytochrome c oxidase I is the main subunit of the cytochrome c oxidase complex. Mutations in MT-CO1 have been associated with Leber's hereditary optic neuropathy (LHON), acquired idiopathic sideroblastic anemia, Complex IV deficiency, colorectal cancer, sensorineural deafness, and recurrent myoglobinuria.1occ: STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE1oco: BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE1ocr: BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE1ocz: BOVINE HEART CYTOCHROME C OXIDASE IN AZIDE-BOUND STATE1v54: Bovine heart cytochrome c oxidase at the fully oxidized state1v55: Bovine heart cytochrome c oxidase at the fully reduced state2dyr: Bovine heart cytochrome C oxidase at the fully oxidized state2dys: Bovine heart cytochrome C oxidase modified by DCCD2eij: Bovine heart cytochrome C oxidase in the fully reduced state2eik: Cadmium ion binding structure of bovine heart cytochrome C oxidase in the fully reduced state2eil: Cadmium ion binding structure of bovine heart cytochrome C oxidase in the fully oxidized state2eim: Zinc ion binding structure of bovine heart cytochrome C oxidase in the fully reduced state2ein: Zinc ion binding structure of bovine heart cytochrome C oxidase in the fully oxidized state2occ: BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE Cytochrome c oxidase I (COX1) also known as mitochondrially encoded cytochrome c oxidase I (MT-CO1) is a protein that in humans is encoded by the MT-CO1 gene. In other eukaryotes, the gene is called COX1, CO1, or COI. Cytochrome c oxidase I is the main subunit of the cytochrome c oxidase complex. Mutations in MT-CO1 have been associated with Leber's hereditary optic neuropathy (LHON), acquired idiopathic sideroblastic anemia, Complex IV deficiency, colorectal cancer, sensorineural deafness, and recurrent myoglobinuria. One of 37 mitochondrial genes, the MT-CO1 gene is located from nucleotide pairs 5904 to 7444 on the guanine-rich heavy (H) section of mtDNA. The gene product is a 57 kDa protein composed of 513 amino acids. 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. Cytochrome c oxidase (EC 1.9.3.1) 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 (EC 1.10.3.10), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian 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. In contrast to eukaryotes the respiratory chain of prokaryotes is branched to multiple terminal oxidases. 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. It has been shown that eubacterial quinol oxidase was derived from cytochrome c oxidase in Gram-positive bacteria and that archaebacterial quinol oxidase has an independent origin. A considerable amount of evidence suggests that proteobacteria (Purple bacteria) acquired quinol oxidase through a lateral gene transfer from Gram-positive bacteria. A related nitric-oxide reductase (EC 1.7.99.7) exists in denitrifying species of archaea and eubacteria and is a heterodimer of cytochromes b and c. Phenazine methosulphate can act as acceptor. It has been suggested that cytochrome c oxidase catalytic subunits evolved from ancient nitric oxide reductases that could reduce both nitrogen and oxygen. Mutations in this gene are associated with Leber's hereditary optic neuropathy (LHON), acquired idiopathic sideroblastic anemia, Complex IV deficiency, colorectal cancer, sensorineural deafness, and recurrent myoglobinuria. LHON, correlated with mutations in MT-CO1, is characterized by optic nerve dysfunction, causing subacute or acute central vision loss. Some patients may display neurological or cardiac conduction defects. Because this disease is a result of mitochondrial DNA mutations affecting the respiratory chain complexes, it is inherited maternally.