ArticleFree radical biology & medicine2010
Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage.
Article in Free radical biology & medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia.International journal of molecular sciences · 2023Review
- Advances in Postharvest Storage and Preservation Strategies forFoods (Basel, Switzerland) · 2023Review
- Addressing the Neuroprotective Actions of Coffee in Parkinson's Disease: An Emerging Nutrigenomic Analysis.Antioxidants (Basel, Switzerland) · 2022Review
- p66Shc in Cardiovascular Pathology.Cells · 2022Review
- ROS Defense Systems and Terminal Oxidases in Bacteria.Antioxidants (Basel, Switzerland) · 2021Review
- Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of CytochromeOxidative medicine and cellular longevity · 2020Review
- High Temperature Induced Anthocyanin Inhibition and Active Degradation inFrontiers in plant science · 2017Article
- How hydrogen peroxide is metabolized by oxidized cytochrome c oxidase.Biochemistry · 2014Article
- Elucidating the mechanism of ferrocytochrome c heme disruption by peroxidized cardiolipin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Removal of H₂O₂ and generation of superoxide radical: role of cytochrome c and NADH.Free radical biology & medicine · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
An excess of ferricytochrome c protects purified mitochondrial cytochrome c oxidase and bound cardiolipin from hydrogen peroxide-induced oxidative modification. All of the peroxide-induced changes within cytochrome c oxidase, such as oxidation of Trp(19,IV) and Trp(48,VIIc), partial dissociation of subunits VIa and VIIa, and generation of cardiolipin hydroperoxide, no longer take place in the presence of ferricytochrome c. Furthermore, ferricytochrome c suppresses the yield of H(2)O(2)-induced free radical detectable by electron paramagnetic resonance spectroscopy within cytochrome c oxidase. These protective effects are based on two mechanisms. The first involves the peroxidase/catalase-like activity of ferricytochrome c, which results in the decomposition of H(2)O(2), with the apparent bimolecular rate constant of 5.1±1.0M(-1)s(-1). Although this value is lower than the rate constant of a specialized peroxidase, the activity is sufficient to eliminate H(2)O(2)-induced damage to cytochrome c oxidase in the presence of an excess of ferricytochrome c. The second mechanism involves ferricytochrome c-induced quenching of free radicals generated within cytochrome c oxidase. These results suggest that ferricytochrome c may have an important role in protection of cytochrome c oxidase and consequently the mitochondrion against oxidative damage.
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Registered trials
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