ArticleThe Journal of biological chemistry2014
Identification of redox partners and development of a novel chimeric bacterial nitric oxide synthase for structure activity analyses.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Diuretic and Anti-hyperuricemic Effects of Geranyl Acetate in Rats.Current medicinal chemistry · 2026Article
- Redox Properties ofInternational journal of molecular sciences · 2024Article
- The Response ofJournal of bacteriology · 2019Article
- Article
- Inhibitor Bound Crystal Structures of Bacterial Nitric Oxide Synthase.Biochemistry · 2015Article
- Nitric Oxide Synthase as a Target for Methicillin-Resistant Staphylococcus aureus.Chemistry & biology · 2015Article
- Structure-based design of bacterial nitric oxide synthase inhibitors.Journal of medicinal chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Production of nitric oxide (NO) by nitric oxide synthase (NOS) requires electrons to reduce the heme iron for substrate oxidation. Both FAD and FMN flavin groups mediate the transfer of NADPH derived electrons to NOS. Unlike mammalian NOS that contain both FAD and FMN binding domains within a single polypeptide chain, bacterial NOS is only composed of an oxygenase domain and must rely on separate redox partners for electron transfer and subsequent activity. Here, we report on the native redox partners for Bacillus subtilis NOS (bsNOS) and a novel chimera that promotes bsNOS activity. By identifying and characterizing native redox partners, we were also able to establish a robust enzyme assay for measuring bsNOS activity and inhibition. This assay was used to evaluate a series of established NOS inhibitors. Using the new assay for screening small molecules led to the identification of several potent inhibitors for which bsNOS-inhibitor crystal structures were determined. In addition to characterizing potent bsNOS inhibitors, substrate binding was also analyzed using isothermal titration calorimetry giving the first detailed thermodynamic analysis of substrate binding to NOS.
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Registered trials
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