Biochemical and crystallographic studies of monomeric and dimeric bovine cytochrome c oxidase.
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ABSTRACT: Cytochrome c oxidase (CcO), a terminal oxidase in the respiratory chain, catalyzes the reduction of O2 to water coupled with the proton pump across the membrane. Mitochondrial CcO exists in monomeric and dimeric forms, and as a monomer as part of the respiratory supercomplex, although the enzymatic reaction proceeds in the CcO monomer. Recent biochemical and crystallographic studies of monomeric and dimeric CcOs have revealed functional and structural differences among them. In solubilized mitochondrial membrane, the monomeric form is dominant, and a small amount of dimer is observed. The activity of the monomeric CcO is higher than that of the dimer, suggesting that the monomer is the active form. In the structure of monomeric CcO, a hydrogen bond network of water molecu
SUBMITTER: Shinzawa-Itoh K
PROVIDER: S-EPMC8390318 | biostudies-literature | 2021
REPOSITORIES: biostudies-literature
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