ArticleACS catalysis2018
Spectroscopy and DFT Calculations of Flavo-Diiron Nitric Oxide Reductase Identify Bridging Structures of NO-Coordinated Diiron Intermediates.
Article in ACS catalysis, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Hydroxo-bridged active site of flavodiiron NO reductase revealed by NRVS and DFT.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Electronic Modification of a Reduced Mononuclear Nonheme Iron Nitrosyl Complex Leads to HNO Release.Journal of the American Chemical Society · 2025Article
- Reductive Coupling of Nitric Oxide by Cu(I): Stepwise Formation of Mono- and Dinitrosyl SpeciesJournal of the American Chemical Society · 2023Article
- Particle Swarm Fitting of Spin Hamiltonians: Magnetic Circular Dichroism of Reduced and NO-Bound Flavodiiron Protein.Inorganic chemistry · 2022Article
- A Nonheme Mononuclear {FeNO}Angewandte Chemie (International ed. in English) · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.Chemical reviews · 2020Review
- Copper(I) Complex Mediated Nitric Oxide Reductive Coupling: Ligand Hydrogen Bonding Derived Proton Transfer Promotes NJournal of the American Chemical Society · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Flavo-diiron proteins (FDPs) are widespread in anaerobic bacteria, archaea, and protozoa, where they serve as the terminal components of dioxygen and nitric oxide reductive scavenging pathways. FDPs contain an N,O-ligated diiron site adjacent to a flavin mononucleotide (FMN) cofactor. The diiron site is structurally similar to those in hemerythrin, ribonucleotide reductase, and methane monooxygenase. However, only FDPs turn over NO to N
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