ArticleThe Journal of biological chemistry2017
A Two-component NADPH Oxidase (NOX)-like System in Bacteria Is Involved in the Electron Transfer Chain to the Methionine Sulfoxide Reductase MsrP.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Where metabolism and virulence meet-sulfoxide reductases as determinants of bacterial survival.Biochemical Society transactions · 2026Review
- Studies of the membrane-bound flavocytochrome MsrQ flavin mononucleotide (FMN)-binding site reveal an unexpected ubiquinone cofactor.The FEBS journal · 2025Article
- Bacteria detect neutrophils via a system that responds to hypochlorous acid and flow.bioRxiv : the preprint server for biology · 2025Article
- Article
- A high-throughput and low-waste viability assay for microbes.Nature microbiology · 2023Article
- Article
- A Year at the Forefront of Bacterial Defense Systems Against Neutrophilic Oxidants.Biology open · 2023Article
- Transcriptomic and phenotype analysis revealed the role ofFrontiers in cellular and infection microbiology · 2023Article
- A Large-Scale Multiple Genome Comparison of Acidophilic Archaea (pH ≤ 5.0) Extends Our Understanding of Oxidative Stress Responses in Polyextreme Environments.Antioxidants (Basel, Switzerland) · 2021Article
- Draft Genome Sequences ofMicrobiology resource announcements · 2021Article
- NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology.Antioxidants (Basel, Switzerland) · 2021Review
- Article
- Microbial ingress andBioactive materials · 2020Article
- An approach to the photocatalytic mechanism in the TiOApplied catalysis. B, Environmental · 2020Review
- Interdomain Flexibility within NADPH Oxidase Suggested by SANS Using LMNG Stealth Carrier.Biophysical journal · 2020Article
- Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.Metal ions in life sciences · 2020Article
- Molecular Mechanisms Underpinning Aggregation inMicroorganisms · 2020Article
- Addressing Ligand-Based Redox in Molybdenum-Dependent Methionine Sulfoxide Reductase.Journal of the American Chemical Society · 2020Article
- Methionine Sulfoxide Reductases of Archaea.Antioxidants (Basel, Switzerland) · 2018Review
- Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MsrPQ is a newly identified methionine sulfoxide reductase system found in bacteria, which appears to be specifically involved in the repair of periplasmic proteins oxidized by hypochlorous acid. It involves two proteins: a periplasmic one, MsrP, previously named YedY, carrying out the Msr activity, and MsrQ, an integral b-type heme membrane-spanning protein, which acts as the specific electron donor to MsrP. MsrQ, previously named YedZ, was mainly characterized by bioinformatics as a member of the FRD superfamily of heme-containing membrane proteins, which include the NADPH oxidase proteins (NOX/DUOX). Here we report a detailed biochemical characterization of the MsrQ protein from
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