ArticleJournal of the American Chemical Society2014
Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Ligand Radicals Tune LPMO Activity in Model Complex.Inorganic chemistry · 2026Article
- A Post-translational Histidine-Histidine Cross-Link Enhances Enzymatic Oxygen Reduction Activity with Greater pH Adaptability.Journal of the American Chemical Society · 2025Article
- Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.Biochemistry · 2023Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Effect of myoglobin, hemin, and ferric iron on quality of chicken breast meat.Animal bioscience · 2021Article
- Repurposing metalloproteins as mimics of natural metalloenzymes for small-molecule activation.Journal of inorganic biochemistry · 2021Review
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors.Accounts of chemical research · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.Angewandte Chemie (International ed. in English) · 2017Article
- Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Israel journal of chemistry · 2016Article
- Design and engineering of artificial oxygen-activating metalloenzymes.Chemical Society reviews · 2016Review
- Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.Journal of the American Chemical Society · 2016Article
- Design of Heteronuclear Metalloenzymes.Methods in enzymology · 2016Article
- Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.The Journal of chemical physics · 2015Article
- A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme.Journal of the American Chemical Society · 2015Article
- Defining the role of tyrosine and rational tuning of oxidase activity by genetic incorporation of unnatural tyrosine analogs.Journal of the American Chemical Society · 2015Article
- Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin.Journal of the American Chemical Society · 2014Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Tyrosine is a conserved redox-active amino acid that plays important roles in heme-copper oxidases (HCO). Despite the widely proposed mechanism that involves a tyrosyl radical, its direct observation under O2 reduction conditions remains elusive. Using a functional oxidase model in myoglobin called F33Y-Cu(B)Mb that contains an engineered tyrosine, we report herein direct observation of a tyrosyl radical during both reactions of H2O2 with oxidized protein and O2 with reduced protein by electron paramagnetic resonance spectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.
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