File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Evidence for the Prerequisite Formation of Phenoxyl Radicals in Radical‐Mediated Peptide Tyrosine Nitration In Vacuo

TitleEvidence for the Prerequisite Formation of Phenoxyl Radicals in Radical‐Mediated Peptide Tyrosine Nitration In Vacuo
Authors
Keywordsisomerization
nitration
radical reactions
reaction mechanisms
regioselectivity
Issue Date2020
PublisherWiley - VCH Verlag GmbH & Co. KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/chemistry
Citation
Chemistry - A European Journal, 2020, v. 26 n. 1, p. 331-335 How to Cite?
AbstractThe elementary mechanism of radical‐mediated peptide tyrosine nitration, which is a hallmark of post‐translational modification of proteins under nitrative stress in vivo, has been elucidated in detail by using an integrated approach that combines the gas‐phase synthesis of prototypical molecular tyrosine‐containing peptide radical cations, ion–molecule reactions, and isotopic labeling experiments with DFT calculations. This reaction first involves the radical recombination of .NO2 towards the prerequisite phenoxyl radical tautomer of a tyrosine residue, followed by proton rearrangements, finally yielding the stable and regioselective 3‐nitrotyrosyl residue product. In contrast, nitration with the π‐phenolic radical cation tautomer is inefficient. This first direct experimental evidence for the elementary steps of the radical‐mediated tyrosine nitration mechanism in the gas phase provides a fundamental insight into the regioselectivity of biological tyrosine ortho ‐nitration.
Persistent Identifierhttp://hdl.handle.net/10722/282881
ISSN
2023 Impact Factor: 3.9
2023 SCImago Journal Rankings: 1.058
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorlai, CK-
dc.contributor.authorTang, WK-
dc.contributor.authorSiu, CK-
dc.contributor.authorChu, IK-
dc.date.accessioned2020-06-05T06:22:40Z-
dc.date.available2020-06-05T06:22:40Z-
dc.date.issued2020-
dc.identifier.citationChemistry - A European Journal, 2020, v. 26 n. 1, p. 331-335-
dc.identifier.issn0947-6539-
dc.identifier.urihttp://hdl.handle.net/10722/282881-
dc.description.abstractThe elementary mechanism of radical‐mediated peptide tyrosine nitration, which is a hallmark of post‐translational modification of proteins under nitrative stress in vivo, has been elucidated in detail by using an integrated approach that combines the gas‐phase synthesis of prototypical molecular tyrosine‐containing peptide radical cations, ion–molecule reactions, and isotopic labeling experiments with DFT calculations. This reaction first involves the radical recombination of .NO2 towards the prerequisite phenoxyl radical tautomer of a tyrosine residue, followed by proton rearrangements, finally yielding the stable and regioselective 3‐nitrotyrosyl residue product. In contrast, nitration with the π‐phenolic radical cation tautomer is inefficient. This first direct experimental evidence for the elementary steps of the radical‐mediated tyrosine nitration mechanism in the gas phase provides a fundamental insight into the regioselectivity of biological tyrosine ortho ‐nitration.-
dc.languageeng-
dc.publisherWiley - VCH Verlag GmbH & Co. KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/chemistry-
dc.relation.ispartofChemistry - A European Journal-
dc.rightsThis is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.-
dc.subjectisomerization-
dc.subjectnitration-
dc.subjectradical reactions-
dc.subjectreaction mechanisms-
dc.subjectregioselectivity-
dc.titleEvidence for the Prerequisite Formation of Phenoxyl Radicals in Radical‐Mediated Peptide Tyrosine Nitration In Vacuo-
dc.typeArticle-
dc.identifier.emailChu, IK: ivankchu@hkucc.hku.hk-
dc.identifier.authorityChu, IK=rp00683-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/chem.201904484-
dc.identifier.pmid31657861-
dc.identifier.scopuseid_2-s2.0-85075974490-
dc.identifier.hkuros310233-
dc.identifier.volume26-
dc.identifier.issue1-
dc.identifier.spage331-
dc.identifier.epage335-
dc.identifier.isiWOS:000498463000001-
dc.publisher.placeGermany-
dc.identifier.issnl0947-6539-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats