ArticleNature chemistry2016
A motif for reversible nitric oxide interactions in metalloenzymes.
Article in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Electronic Modification of a Reduced Mononuclear Nonheme Iron Nitrosyl Complex Leads to HNO Release.Journal of the American Chemical Society · 2025Article
- Copper sulfide mineral performs non-enzymatic anaerobic ammonium oxidation through a hydrazine intermediate.Nature chemistry · 2024Article
- Cluster dynamics of heterometallic trinuclear clusters during ligand substitution, redox chemistry, and group transfer processes.Chemical science · 2024Article
- Primary and Secondary Coordination Sphere Effects on the Structure and Function ofJournal of the American Chemical Society · 2023Article
- Unraveling the Molecular Mechanism ofInorganic chemistry · 2023Article
- Acid-induced nitrite reduction of nonheme iron(ii)-nitrite: mimicking biological Fe-NiR reactions.Chemical science · 2023Article
- Influence of the primary and secondary coordination spheres on nitric oxide adsorption and reactivity in cobalt(ii)-triazolate frameworks.Chemical science · 2021Article
- Plant Nitric Oxide Signaling under Drought Stress.Plants (Basel, Switzerland) · 2021Review
- Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.Journal of the American Chemical Society · 2020Article
- Lewis Acid Coordination Redirects S-Nitrosothiol Signaling Output.Angewandte Chemie (International ed. in English) · 2020Article
- Crystal-facet-dependent denitrosylation: modulation of NO release fromChemical science · 2019Article
- Methylated Histidines Alter Tautomeric Preferences that Influence the Rates of Cu Nitrite Reductase Catalysis in Designed Peptides.Journal of the American Chemical Society · 2019Article
- Metalloproteins: A switch for blue copper proteins?Nature chemistry · 2016Article
Corrections and comments
- Commented on byNow we NO.2016
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitric oxide (NO) participates in numerous biological processes, such as signalling in the respiratory system and vasodilation in the cardiovascular system. Many metal-mediated processes involve direct reaction of NO to form a metal-nitrosyl (M-NO), as occurs at the Fe(2+) centres of soluble guanylate cyclase or cytochrome c oxidase. However, some copper electron-transfer proteins that bear a type 1 Cu site (His2Cu-Cys) reversibly bind NO by an unknown motif. Here, we use model complexes of type 1 Cu sites based on tris(pyrazolyl)borate copper thiolates [Cu(II)]-SR to unravel the factors involved in NO reactivity. Addition of NO provides the fully characterized S-nitrosothiol adduct [Cu(I)](κ(1)-N(O)SR), which reversibly loses NO on purging with an inert gas. Computational analysis outlines a low-barrier pathway for the capture and release of NO. These findings suggest a new motif for reversible binding of NO at bioinorganic metal centres that can interconvert NO and RSNO molecular signals at copper sites.
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Registered trials
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