Membrane-Bound Flavocytochrome MsrQ Is a Substrate of the Flavin Reductase Fre in
Journal
ACS chemical biology
ISSN: 1554-8937
Titre abrégé: ACS Chem Biol
Pays: United States
ID NLM: 101282906
Informations de publication
Date de publication:
19 11 2021
19 11 2021
Historique:
pubmed:
23
9
2021
medline:
1
2
2022
entrez:
22
9
2021
Statut:
ppublish
Résumé
MsrPQ is a new type of methionine sulfoxide reductase (Msr) system found in bacteria. It is specifically involved in the repair of periplasmic methionine residues that are oxidized by hypochlorous acid. MsrP is a periplasmic molybdoenzyme that carries out the Msr activity, whereas MsrQ, an integral membrane-bound hemoprotein, acts as the physiological partner of MsrP to provide electrons for catalysis. Although MsrQ (YedZ) was associated since long with a protein superfamily named FRD (ferric reductase domain), including the eukaryotic NADPH oxidases and STEAP proteins, its biochemical properties are still sparsely documented. Here, we have investigated the cofactor content of the
Identifiants
pubmed: 34550690
doi: 10.1021/acschembio.1c00613
doi:
Substances chimiques
Enzymes
0
Escherichia coli Proteins
0
Membrane Proteins
0
Flavin Mononucleotide
7N464URE7E
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM