ArticleJournal of the American Chemical Society2012
Two tyrosyl radicals stabilize high oxidation states in cytochrome C oxidase for efficient energy conservation and proton translocation.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Carbon Monoxide and Prokaryotic Energy Metabolism.International journal of molecular sciences · 2025Review
- Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025Review
- Heme-copper and Heme OJournal of inorganic biochemistry · 2023Review
- Study and design of amino acid-based radical enzymes using unnatural amino acids.RSC chemical biology · 2023Article
- Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.Biochemistry · 2023Article
- Reaction pathways, proton transfer, and proton pumping in ba3 class cytochrome c oxidase: perspectives from DFT quantum chemistry and molecular dynamics.Frontiers in chemistry · 2023Article
- Radical in the Peroxide-Produced F-Type Ferryl Form of Bovine CytochromeInternational journal of molecular sciences · 2022Article
- The three-spin intermediate at the O-O cleavage and proton-pumping junction in heme-Cu oxidases.Science (New York, N.Y.) · 2021Article
- Structural and Biochemical Characterization of a Dye-Decolorizing Peroxidase fromInternational journal of molecular sciences · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine.iScience · 2020Review
- Coupled transport of electrons and protons in a bacterial cytochromePhysical chemistry chemical physics : PCCP · 2020Article
- Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in CytochromeJournal of the American Chemical Society · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.Biochemistry · 2018Article
- Pourbaix Diagram, Proton-Coupled Electron Transfer, and Decay Kinetics of a Protein Tryptophan Radical: Comparing the Redox Properties of WJournal of the American Chemical Society · 2018Article
- Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.Journal of the American Chemical Society · 2017Article
- Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.Journal of the American Chemical Society · 2016Article
- Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?Quarterly reviews of biophysics · 2015Review
- Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
The reaction of oxidized bovine cytochrome c oxidase (bCcO) with hydrogen peroxide (H(2)O(2)) was studied by electron paramagnetic resonance (EPR) to determine the properties of radical intermediates. Two distinct radicals with widths of 12 and 46 G are directly observed by X-band EPR in the reaction of bCcO with H(2)O(2) at pH 6 and pH 8. High-frequency EPR (D-band) provides assignments to tyrosine for both radicals based on well-resolved g-tensors. The wide radical (46 G) exhibits g-values similar to a radical generated on L-Tyr by UV-irradiation and to tyrosyl radicals identified in many other enzyme systems. In contrast, the g-values of the narrow radical (12 G) deviate from L-Tyr in a trend akin to the radicals on tyrosines with substitutions at the ortho position. X-band EPR demonstrates that the two tyrosyl radicals differ in the orientation of their β-methylene protons. The 12 G wide radical has minimal hyperfine structure and can be fit using parameters unique to the post-translationally modified Y244 in bCcO. The 46 G wide radical has extensive hyperfine structure and can be fit with parameters consistent with Y129. The results are supported by mixed quantum mechanics and molecular mechanics calculations. In addition to providing spectroscopic evidence of a radical formed on the post-translationally modified tyrosine in CcO, this study resolves the much debated controversy of whether the wide radical seen at low pH in the bovine enzyme is a tyrosine or tryptophan. The possible role of radical formation and migration in proton translocation is discussed.
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