ArticleBiochimica et biophysica acta2011
Topography of tyrosine residues and their involvement in peroxidation of polyunsaturated cardiolipin in cytochrome c/cardiolipin peroxidase complexes.
Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Tyrosine 48 Phosphorylation of CytochromeBiomolecules · 2026Article
- Tyrosine 67 Phosphorylation Controls Respiration and Limits the Apoptotic Functions of CytochromeCells · 2025Article
- Cardiac Tyrosine 97 Phosphorylation of CytochromeInternational journal of molecular sciences · 2025Article
- Order-to-Disorder and Disorder-to-Order Transitions of Proteins upon Binding to Phospholipid Membranes: Common Ground and Dissimilarities.Biomolecules · 2025Review
- Mechanisms of mitochondrial damage-associated molecular patterns associated with inflammatory response in cardiovascular diseases.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025Review
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Cardiolipin Membranes Promote CytochromeMolecules (Basel, Switzerland) · 2024Article
- Redox Pioneer: Professor Valerian Kagan.Antioxidants & redox signaling · 2022Article
- The effect of cardiolipin side chain composition on cytochrome c protein conformation and peroxidase activity.Physiological reports · 2021Article
- Cytochrome c phosphorylation: Control of mitochondrial electron transport chain flux and apoptosis.The international journal of biochemistry & cell biology · 2020Article
- Redox phospholipidomics of enzymatically generated oxygenated phospholipids as specific signals of programmed cell death.Free radical biology & medicine · 2020Review
- Redox Epiphospholipidome in Programmed Cell Death Signaling: Catalytic Mechanisms and Regulation.Frontiers in endocrinology · 2020Review
- Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics.Structure (London, England : 1993) · 2019Article
- Tissue-specific regulation of cytochrome c by post-translational modifications: respiration, the mitochondrial membrane potential, ROS, and apoptosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Review
- "Only a Life Lived for Others Is Worth Living": Redox Signaling by Oxygenated Phospholipids in Cell Fate Decisions.Antioxidants & redox signaling · 2018Review
- Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control.Molecules (Basel, Switzerland) · 2018Review
- Relating the multi-functionality of cytochrome c to membrane binding and structural conversion.Biophysical reviews · 2018Review
- The Cytotoxic Action of Cytochrome C/Cardiolipin Nanocomplex (Cyt-CL) on Cancer Cells in Culture.Pharmaceutical research · 2017Article
- Known unknowns of cardiolipin signaling: The best is yet to come.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Journal of the American Chemical Society · 2016Article
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15 authors.
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Abstract
Formation of cytochrome c (cyt c)/cardiolipin (CL) peroxidase complex selective toward peroxidation of polyunsaturated CLs is a pre-requisite for mitochondrial membrane permeabilization. Tyrosine residues - via the generation of tyrosyl radicals (Tyr) - are likely reactive intermediates of the peroxidase cycle leading to CL peroxidation. We used mutants of horse heart cyt c in which each of the four Tyr residues was substituted for Phe and assessed their contribution to the peroxidase catalysis. Tyr67Phe mutation was associated with a partial loss of the oxygenase function of the cyt c/CL complex and the lowest concentration of H(2)O(2)-induced Tyr radicals in electron paramagnetic resonance (EPR) spectra. Our MS experiments directly demonstrated decreased production of CL-hydroperoxides (CL-OOH) by Tyr67Phe mutant. Similarly, oxidation of a phenolic substrate, Amplex Red, was affected to a greater extent in Tyr67Phe than in three other mutants. Tyr67Phe mutant exerted high resistance to H(2)O(2)-induced oligomerization. Measurements of Tyr fluorescence, hetero-nuclear magnetic resonance (NMR) and computer simulations position Tyr67 in close proximity to the porphyrin ring heme iron and one of the two axial heme-iron ligand residues, Met80. Thus, the highly conserved Tyr67 is a likely electron-donor (radical acceptor) in the oxygenase half-reaction of the cyt c/CL peroxidase complex.
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