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Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. Zusätzlich bieten wir Ihnen Cytochrome C Oxidase Subunit VIa Polypeptide 1 Antikörper (77) und und viele weitere Produktgruppen zu diesem Protein an.
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We demonstrate a developmental isoform switch of COX6A and COX7A subunits in human and mouse skeletal muscle
Mutation of COX6A1 causes a recessive axonal or mixed form of Charcot-Marie-Tooth disease.
Novel insights into the assembly and function of human nuclear-encoded cytochrome c oxidase subunits 6a
Data found that subunits Cox6a, Cox6b and Cox7a assembled into pre-existing complex IV, while Cox4-1 and Cox6c subunits assembled into subcomplexes that may represent rate-limiting intermediates.
COX6A1 was identified as the protein that inhibits yeast cells Bax-sensitivity and protects mammalian cells from 4-HPR-induced apoptosis.
Loss of COX6A1 causes a recessive axonal or mixed form of Charcot-Marie-Tooth disease.
After copper is reduced, electron transfer to oxidized heme a(3) is enhanced relative to the rate of entry of the first electron.
photoreduction of oxidized bovine heart cytochrome c oxidase (CcO) by visible and UV radiation was investigated in the absence and presence of external reagents
The calculations reported here show substantial protonation of Lys(I)-319 of cytochrome c oxidase at neutral pH once the stable X-ray crystallographic water molecule found immediately next to it is treated explicitly.
X-ray structures of bovine heart cytochrome c oxidase at 1.8/1.9 A resolution in the oxidized/reduced states exhibit a redox coupled conformational change of an aspartate located near the intermembrane surface of the enzyme.
The P(M)-->F transition of the catalytic cycle of cytochrome c oxidase from bovine heart was investigated using single-electron photoreduction and monitoring the subsequent events using spectroscopic and electometric techniques.
Extended x-ray absorption spectroscopy analysis of Zn binding site(s) in bovine-heart cytochrome c oxidase and characterization of the inhibitory effect of internal zinc on respiratory activity and proton pumping reconstituted oxidase are presented.
perturbation of an arginine guanidinium, probably Arg-438, lowers the energy of the transient charge-uncompensated electron-transfer intermediate by changing the charge distribution in response to heme-heme electron transfer
analysis of the peroxidase activity of mitochondrial cytochrome c oxidase peroxidase activity
The conserved glutamic acid 242 near the active site of CcO undergoes a protonation state-dependent conformational change, which provides a valve in the pumping mechanism.
Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in the electron transfer and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes polypeptide 1 (liver isoform) of subunit VIa, and polypeptide 1 is found in all non-muscle tissues. Polypeptide 2 (heart/muscle isoform) of subunit VIa is encoded by a different gene, and is present only in striated muscles. These two polypeptides share 66% amino acid sequence identity. It has been reported that there may be several pseudogenes on chromosomes 1, 6, 7q21, 7q31-32 and 12. However, only one pseudogene (COX6A1P) on chromosome 1p31.1 has been documented.
cytochrome c oxidase polypeptide VIa-liver
, cytochrome c oxidase subunit 6A1, mitochondrial
, COX VIa-L
, cytochrome C oxidase subunit VIa homolog
, cytochrome c oxidase subunit VIA-liver
, subunit VIaL (liver-type)
, cytochrome c oxidase subunit SSG
, cytochrome-c oxidase
, Cytochrome c oxidase subunit VIa (liver)