ArticleJournal of applied physiology (Bethesda, Md. : 1985)2014
Mitochondrial cytochrome c oxidase: mechanism of action and role in regulating oxidative phosphorylation.
Article in Journal of applied physiology (Bethesda, Md. : 1985), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
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- Ultra-High Dose Rate FLASH Irradiation Induced Radio-Resistance of Normal Fibroblast Cells Can Be Enhanced by Hypoxia and Mitochondrial Dysfunction Resulting From Loss of Cytochrome C.Frontiers in cell and developmental biology · 2021Article
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- A neuroglobin-based high-affinity ligand trap reverses carbon monoxide-induced mitochondrial poisoning.The Journal of biological chemistry · 2020Article
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- The Central Role of Glucokinase in Glucose Homeostasis: A Perspective 50 Years After Demonstrating the Presence of the Enzyme in Islets of Langerhans.Frontiers in physiology · 2019Review
- Intracardiac light catheter for rapid scanning transmural absorbance spectroscopy of perfused myocardium: measurement of myoglobin oxygenation and mitochondria redox state.American journal of physiology. Heart and circulatory physiology · 2017Article
- Oxidative phosphorylation: regulation and role in cellular and tissue metabolism.The Journal of physiology · 2017Review
- Phenotypes, antioxidant responses, and gene expression changes accompanying a sugar-only diet in Bactrocera dorsalis (Hendel) (Diptera: Tephritidae).BMC evolutionary biology · 2017Article
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- Phenotypic plasticity, trade-offs and gene expression changes accompanying dietary restriction and switches in Bactrocera dorsalis (Hendel) (Diptera: Tephritidae).Scientific reports · 2017Article
- Modeling the detailed kinetics of mitochondrial cytochrome c oxidase: Catalytic mechanism and nitric oxide inhibition.Journal of applied physiology (Bethesda, Md. : 1985) · 2016Article
- Lysyl Oxidase Isoforms and Potential Therapeutic Opportunities for Fibrosis and Cancer.Expert opinion on therapeutic targets · 2016Review
- Mitochondrial cytochrome c oxidase: Mechanism of action and role in regulating oxidative phosphorylation: Reply to Pannala, Beard, and Dash.Journal of applied physiology (Bethesda, Md. : 1985) · 2015Article
Corrections and comments
- Commented on by
- Commented on by
- Erratum issuedCorrigendum.2015
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial oxidative phosphorylation has a central role in eukaryotic metabolism, providing the energy (ATP) required for survival. Regulation of this important pathway is, however, still not understood, largely due to limitations in the ability to measure the essential metabolites, including oxygen (pO2, oxygen pressure), ADP, and AMP. In addition, neither the mechanism of oxygen reduction by mitochondrial cytochrome c oxidase nor how its rate is controlled is understood, although this enzyme determines the rate of oxygen consumption and thereby the rate of ATP synthesis. Cytochrome c oxidase is responsible for reduction of molecular oxygen to water using reducing equivalents donated by cytochrome c and for site 3 energy coupling in oxidative phosphorylation. A mechanism-based model of the cytochrome c oxidase reaction is presented in which transfer of reducing equivalents from the lower- to the higher-potential region of the coupling site occurs against an opposing energy barrier, Q. The steady-state rate equation is fitted to data for the dependence of mitochondrial respiratory rate on cytochrome c reduction, oxygen pressure (pO2), and [ATP]/[ADP][Pi] at pH 6.5 to 8.35 (where Pi is inorganic phosphate). The fit of the rate expression to the experimental data is very good for all experimental conditions. Levels of the intermediates in oxygen reduction in the oxidase reaction site have been calculated. An intermediate in the reaction, tentatively identified as peroxide, bridged between the iron and copper atoms of the reaction site has a central role in coupling mitochondrial respiration to the [ATP]/[ADP][Pi].
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