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
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

Pagination

2547-2559

Auteurs

Christelle Caux (C)

CNRS, CEA, IRIG-LCBM, Laboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, Grenoble 38054, France.

Bruno Guigliarelli (B)

CNRS, BIP-UMR 7281 Laboratoire de Bioénergétique et Ingénierie des Protéines, Aix-Marseille Univ., Marseille 13402, France.

Corinne Vivès (C)

CNRS, CEA, Institut de Biologie Structurale, Univ. Grenoble Alpes, Grenoble 38044, France.

Frédéric Biaso (F)

CNRS, BIP-UMR 7281 Laboratoire de Bioénergétique et Ingénierie des Protéines, Aix-Marseille Univ., Marseille 13402, France.

Marius Horeau (M)

CNRS, CEA, IRIG-LCBM, Laboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, Grenoble 38054, France.

Hawra Hassoune (H)

CNRS, CEA, IRIG-LCBM, Laboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, Grenoble 38054, France.

Isabelle Petit-Hartlein (I)

CNRS, CEA, Institut de Biologie Structurale, Univ. Grenoble Alpes, Grenoble 38044, France.

Céline Juillan-Binard (C)

CNRS, CEA, Institut de Biologie Structurale, Univ. Grenoble Alpes, Grenoble 38044, France.

Stephane Torelli (S)

CNRS, CEA, IRIG-LCBM, Laboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, Grenoble 38054, France.

Franck Fieschi (F)

CNRS, CEA, Institut de Biologie Structurale, Univ. Grenoble Alpes, Grenoble 38044, France.

Vincent Nivière (V)

CNRS, CEA, IRIG-LCBM, Laboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, Grenoble 38054, France.

Articles similaires

Female Biofilms Animals Lactobacillus Mice
Humans Stomach Neoplasms Macrophages Tumor Microenvironment Disease Progression
Host Specificity Bacteriophages Genomics Algorithms Escherichia coli
Animals Humans TOR Serine-Threonine Kinases Lupus Erythematosus, Systemic Arthritis, Rheumatoid

Classifications MeSH