Characterization of disulfide (cystine) oxidation by HOCl in a model peptide: Evidence for oxygen addition, disulfide bond cleavage and adduct formation with thiols.
Cystine
Disulfide
Glutathionylation
Hypochlorous acid
Oxidation
Protein oxidation
Sulfinic acid
Sulfonic acid
Thiosulfinate
Journal
Free radical biology & medicine
ISSN: 1873-4596
Titre abrégé: Free Radic Biol Med
Pays: United States
ID NLM: 8709159
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
04
03
2020
revised:
20
04
2020
accepted:
24
04
2020
pubmed:
7
5
2020
medline:
22
6
2021
entrez:
7
5
2020
Statut:
ppublish
Résumé
Disulfide bonds play a key role in stabilizing proteins by cross-linking secondary structures. Whilst many disulfides are effectively unreactive, it is increasingly clear that some disulfides are redox active, participate in enzymatic reactions and/or regulate protein function by allosteric mechanisms. Previously (Karimi et al., Sci. Rep. 2016, 6, 38752) we have shown that some disulfides react rapidly with biological oxidants due to favourable interactions with available lone-pairs of electrons. Here we present data from kinetic, mechanistic and product studies for HOCl-mediated oxidation of a protected nine-amino acid model peptide containing a N- to C-terminal disulfide bond. This peptide reacts with HOCl with k
Identifiants
pubmed: 32370994
pii: S0891-5849(20)30541-4
doi: 10.1016/j.freeradbiomed.2020.04.023
pii:
doi:
Substances chimiques
Disulfides
0
Peptides
0
Sulfhydryl Compounds
0
Cystine
48TCX9A1VT
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
62-74Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.