ArticleThe Biochemical journal2020
Structural insights into the mechanism of oxidative activation of heme-free H-NOX from Vibrio cholerae.
Article in The Biochemical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 4 citations in OpenAlex.
- H-NOX and NosP Regulate Flagellar Protein and Virulence Factor Production in Vibrio Cholerae.Molecular & cellular proteomics : MCP · 2026Article
- Oxidative Activation of the Heme Nitric Oxide/Oxygen-Binding Protein (H-NOX) fromBiochemistry · 2025Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
- H-NOX proteins in the virulence of pathogenic bacteria.Bioscience reports · 2022Review
- On or Off: Life-Changing Decisions Made byInfectious microbes & diseases · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial heme nitric oxide/oxygen (H-NOX) domains are nitric oxide (NO) or oxygen sensors. This activity is mediated through binding of the ligand to a heme cofactor. However, H-NOX from Vibrio cholerae (Vc H-NOX) can be easily purified in a heme-free state that is capable of reversibly responding to oxidation, suggesting a heme-independent function as a redox sensor. This occurs by oxidation of Cys residues at a zinc-binding site conserved in a subset of H-NOX homologs. Remarkably, zinc is not lost from the protein upon oxidation, although its ligation environment is significantly altered. Using a combination of computational and experimental approaches, we have characterized localized structural changes that accompany the formation of specific disulfide bonds between Cys residues upon oxidation. Furthermore, the larger-scale structural changes accompanying oxidation appear to mimic those changes observed upon NO binding to the heme-bound form. Thus, Vc H-NOX and its homologs may act as both redox and NO sensors by completely separate mechanisms.
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Registered trials
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