ArticleThe Journal of biological chemistry2009
Superoxide-mediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 53 citations in OpenAlex.
- l-Me-thion-yl-l-tyrosine monohydrate.IUCrData · 2023Article
- Bilirubin Links Heme Metabolism to Neuroprotection by Scavenging Superoxide.Cell chemical biology · 2019Article
- Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration.Redox biology · 2018Review
- Chromophore Renewal and Fluorogen-Binding Tags: A Match Made to Last.Scientific reports · 2017Article
- Activation of dioxygen by copper metalloproteins and insights from model complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Protein oxidation and peroxidation.The Biochemical journal · 2016Review
- Endogenous Generation of Singlet Oxygen and Ozone in Human and Animal Tissues: Mechanisms, Biological Significance, and Influence of Dietary Components.Oxidative medicine and cellular longevity · 2016Review
- Photodynamic therapy: current status and future directions.Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 2015Review
- Real-time measurements of amino acid and protein hydroperoxides using coumarin boronic acid.The Journal of biological chemistry · 2014Article
- Cardiovascular redox and ox stress proteomics.Antioxidants & redox signaling · 2012Review
- Conjugation of glutathione to oxidized tyrosine residues in peptides and proteins.The Journal of biological chemistry · 2012Article
- Urate as a physiological substrate for myeloperoxidase: implications for hyperuricemia and inflammation.The Journal of biological chemistry · 2011Article
- Ribose sugars generate internal glycation cross-links in horse heart myoglobin.Biochemical and biophysical research communications · 2011Article
- Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention.Journal of clinical biochemistry and nutrition · 2011Article
- Tyrosine-lipid peroxide adducts from radical termination: para coupling and intramolecular Diels-Alder cyclization.Journal of the American Chemical Society · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chemistry underlying superoxide toxicity is not fully understood. A potential mechanism for superoxide-mediated injury involves addition to tyrosyl radicals, to give peptide or protein hydroperoxides. The rate constant for the reaction of tyrosyl radicals with superoxide is higher than for dimerization, but the efficiency of superoxide addition to peptides depends on the position of the Tyr residue. We have examined the requirements for superoxide addition and structurally characterized the products for a range of tyrosyl peptides exposed to a peroxidase/O(2)(.) system. These included enkephalins as examples of the numerous proteins and physiological peptides with N-terminal tyrosines. The importance of amino groups in promoting hydroperoxide formation and effect of methionine residues on the reaction were investigated. When tyrosine was N-terminal, the major products were hydroperoxides that had undergone cyclization through conjugate addition of the terminal amine. With non-N-terminal tyrosine, electron transfer from O(2)(.) to the peptide radical prevailed. Peptides containing methionine revealed a novel and efficient intramolecular oxygen transfer mechanism from an initial tyrosine hydroperoxide to give a dioxygenated derivative with one oxygen on the tyrosine and the other forming methionine sulfoxide. Exogenous amines promoted hydroperoxide formation on tyrosyl peptides lacking a terminal amine, without forming an adduct. These findings, plus the high hydroperoxide yields with N-terminal tyrosine, can be explained by a mechanism in which hydrogen bonding of O(2)(.) to the amine increases is oxidizing potential and alters its reactivity. If this amine effect occurred more generally, it could increase the biological reactivity of O(2)(.) and have major implications.
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