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Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. Additionally we are shipping COX17 Antibodies (45) and and many more products for this protein.
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These results collectively indicate that Cox17 might not participate in the action of these anticancer organoruthenium complexes, and further verify the distinct anticancer mechanism of the organoruthenium(II) complexes from cisplatin.
In addition to Atox1, the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (i.e. CCS) and cytochrome c oxidase in mitochondria (i.e. Cox17). [review]
Data show that the redox state of cytochrome c oxidase assembly protein 17 (Cox17), mitochondrial membrane transport protein Mia40 and superoxide dismutase 1 (SOD1) in the cytoplasm were directly observed with in-cell NMR spectroscopy.
Data suggest that Cox17 enhances the reactivity of some platinum/organoplatinum antineoplastic drugs but suppresses the reactivity of at least one platinum antineoplastic drug; glutathione modulates binding of platinum/organoplatinum drugs to Cox17.
CTR1 silencing increased the protein levels of copper chaperone ATOX1 and copper chaperone for superoxide dismutase 1 (CCS-1), but decreased copper chaperone for cytochrome c oxidase (COX17).
Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.
Data imply that up-regulation of COX17 function and increased cytochrome c oxidase activity are frequent features of lung carcinogenesis.
The binding of copper to Cox17 is needed to activate cytochrome c oxidase by Cox17.
Cox17-mediated copper metallation of Sco1, as well as the subsequent failure of Cu(A) site maturation, is the basis for the inefficient assembly of the cytochrome c oxidase complex in SCO1 patients
Cox17 was studied with regard to its expression, purification, and formation of mixed disulfide adducts with sulfhydryl reagents.
XAS (X-ray absorption spectroscopy) determined that Cu4Cox17 contains a Cu4S6-type copper-thiolate cluster, which may provide safe storage of an excess of copper ions
Cu(I)HCox17(2S-S), i.e., the copper-loaded form of the protein, can transfer simultaneously copper(I) and two electrons to the human cochaperone Sco1 (HSco1) in the oxidized state, i.e., with its metal-binding cysteines forming a disulfide bond.
the absence of Cox17 interferes with copper delivery to Cox2, but not to Cox1.
Sp1, NRF-1 and NRF-2 are involved in basal transcription, similar to the transcription mechanism of other CCO-related genes
cox17 has a role in activating cytochrome c oxidase in mice
Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component 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 electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.
COX17 cytochrome c oxidase assembly homolog
, cytochrome c oxidase 17 copper chaperone
, cytochrome c oxidase assembly homolog 17
, cytochrome c oxidase copper chaperone
, human homolog of yeast mitochondrial copper recruitment
, cytochrome c oxidase subunit XVII assembly protein homolog
, cytochrome c oxidase, subunit XVII assembly protein homolog
, COX17 homolog, cytochrome c oxidase assembly protein
, COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)
, COX17 homolog, cytochrome c oxidase assembly protein (yeast)