ArticleBiochemistry2014
How hydrogen peroxide is metabolized by oxidized cytochrome c oxidase.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Copper Drives Remodeling of Metabolic State and Progression of Clear Cell Renal Cell Carcinoma.Cancer discovery · 2025Article
- Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology.Frontiers in chemistry · 2024Review
- Radical in the Peroxide-Produced F-Type Ferryl Form of Bovine CytochromeInternational journal of molecular sciences · 2022Article
- Direct Interaction of Mitochondrial CytochromeCells · 2022Article
- ROS Defense Systems and Terminal Oxidases in Bacteria.Antioxidants (Basel, Switzerland) · 2021Review
- Antidotal effects of methylene blue against cyanide neurological toxicity: in vivo and in vitro studies.Annals of the New York Academy of Sciences · 2020Article
- Antidotal Effects of the Phenothiazine Chromophore Methylene Blue Following Cyanide Intoxication.Toxicological sciences : an official journal of the Society of Toxicology · 2019Article
- Methylene Blue Administration During and After Life-Threatening Intoxication by Hydrogen Sulfide: Efficacy Studies in Adult Sheep and Mechanisms of Action.Toxicological sciences : an official journal of the Society of Toxicology · 2019Article
- Last Word on Viewpoint: Managing the power grid: how myoglobin can regulate PoJournal of applied physiology (Bethesda, Md. : 1985) · 2019Article
- Tumor necrosis factor receptor-associated protein 1 regulates hypoxia-induced apoptosis through a mitochondria-dependent pathway mediated by cytochrome c oxidase subunit II.Burns & trauma · 2019Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
Abstract
In the absence of external electron donors, oxidized bovine cytochrome c oxidase (CcO) exhibits the ability to decompose excess H2O2. Depending on the concentration of peroxide, two mechanisms of degradation were identified. At submillimolar peroxide concentrations, decomposition proceeds with virtually no production of superoxide and oxygen. In contrast, in the millimolar H2O2 concentration range, CcO generates superoxide from peroxide. At submillimolar concentrations, the decomposition of H2O2 occurs at least at two sites. One is the catalytic heme a3-CuB center where H2O2 is reduced to water. During the interaction of the enzyme with H2O2, this center cycles back to oxidized CcO via the intermediate presence of two oxoferryl states. We show that at pH 8.0 two molecules of H2O2 react with the catalytic center accomplishing one cycle. In addition, the reactions at the heme a3-CuB center generate the surface-exposed lipid-based radical(s) that participates in the decomposition of peroxide. It is also found that the irreversible decline of the catalytic activity of the enzyme treated with submillimolar H2O2 concentrations results specifically from the decrease in the rate of electron transfer from heme a to the heme a3-CuB center during the reductive phase of the catalytic cycle. The rates of electron transfer from ferrocytochrome c to heme a and the kinetics of the oxidation of the fully reduced CcO with O2 were not affected in the peroxide-modified CcO.
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Registered trials
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