Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.
Rhodobacter sphaeroides
dimethyl sulfoxide reductase
enzyme kinetics
methionine sulfoxide
oxidative stress
protein oxidation
protein quality control
Journal
Antioxidants (Basel, Switzerland)
ISSN: 2076-3921
Titre abrégé: Antioxidants (Basel)
Pays: Switzerland
ID NLM: 101668981
Informations de publication
Date de publication:
14 Jul 2020
14 Jul 2020
Historique:
received:
10
06
2020
revised:
09
07
2020
accepted:
09
07
2020
entrez:
18
7
2020
pubmed:
18
7
2020
medline:
18
7
2020
Statut:
epublish
Résumé
In proteins, methionine (Met) can be oxidized into Met sulfoxide (MetO). The ubiquitous methionine sulfoxide reductases (Msr) A and B are thiol-oxidoreductases reducing MetO. Reversible Met oxidation has a wide range of consequences, from protection against oxidative stress to fine-tuned regulation of protein functions. Bacteria distinguish themselves by the production of molybdenum-containing enzymes reducing MetO, such as the periplasmic MsrP which protects proteins during acute oxidative stress. The versatile dimethyl sulfoxide (DMSO) reductases were shown to reduce the free amino acid MetO, but their ability to reduce MetO within proteins was never evaluated. Here, using model oxidized proteins and peptides, enzymatic and mass spectrometry approaches, we showed that the
Identifiants
pubmed: 32674377
pii: antiox9070616
doi: 10.3390/antiox9070616
pmc: PMC7402097
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Agence Nationale de la Recherche
ID : METOXIC [ANR 16-CE11-0012]
Organisme : Commissariat à l'Énergie Atomique et aux Énergies Alternatives
ID : Intramural
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