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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. Additionally we are shipping Cytochrome C Oxidase Subunit VIa Polypeptide 1 Antibodies (75) and Cytochrome C Oxidase Subunit VIa Polypeptide 1 Proteins (6) and many more products for this protein.
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 (show CYCS ELISA Kits) oxidase subunits 6a
Data found that subunits Cox6a, Cox6b (show COX6B1 ELISA Kits) and Cox7a (show COX7A1 ELISA Kits) assembled into pre-existing complex IV, while Cox4-1 (show COX4I1 ELISA Kits) and Cox6c (show COX6C ELISA Kits) subunits assembled into subcomplexes that may represent rate-limiting intermediates.
COX6A1 was identified as the protein that inhibits yeast cells Bax (show BAX ELISA Kits)-sensitivity and protects mammalian cells from 4-HPR (show HPR ELISA Kits)-induced apoptosis.
Loss of COX6A1 causes a recessive axonal or mixed form of Charcot-Marie-Tooth disease.
photoreduction of oxidized bovine heart cytochrome c (show CYCS ELISA Kits) oxidase (CcO (show RYR1 ELISA Kits)) by visible and UV radiation was investigated in the absence and presence of external reagents
The calculations reported here show substantial protonation of Lys (show LYZ ELISA Kits)(I)-319 of cytochrome c (show CYCS ELISA Kits) 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 (show CYCS ELISA Kits) 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 (show CYCS ELISA Kits) 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 (show CYCS ELISA Kits) 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 (show CYCS ELISA Kits) oxidase peroxidase activity
The conserved glutamic acid 242 near the active site of CcO (show RYR1 ELISA Kits) 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)