ArticleBiochemistry2010
Insights into the nitric oxide reductase mechanism of flavodiiron proteins from a flavin-free enzyme.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 88 citations in OpenAlex.
- The Role of Iron-Hyponitrite Intermediates in Biology and Insights From Synthetic Model Complexes.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Bimetallic Chemistry by Design: Approaches to the Development of Multifunctional Ligands.Coordination chemistry reviews · 2026Article
- 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
- Isotopic Fractionation and Kinetic Isotope Effects of a Purified Bacterial Nitric Oxide Reductase (NOR).Biochemistry · 2025Article
- 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
- Direct Reduction of NO to NInorganic chemistry · 2022Article
- What Is the Right Level of Activation of a High-Spin {FeNO}Journal of the American Chemical Society · 2022Article
- Bioinspired Di-Fe Complexes: Correlating Structure and Proton Transfer over Four Oxidation States.Journal of the American Chemical Society · 2022Article
- A Nonheme Mononuclear {FeNO}Angewandte Chemie (International ed. in English) · 2021Article
- Tuning metal-metal interactions for cooperative small molecule activation.Chemical communications (Cambridge, England) · 2021Review
- Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers.Journal of the American Chemical Society · 2021Article
- Exploring the Limits of Dative Boratrane Bonding: Iron as a Strong Lewis Base in Low-Valent Non-Heme Iron-Nitrosyl Complexes.Inorganic chemistry · 2020Article
- 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
- Nitric Oxide Reductase Activity in Heme-Nonheme Binuclear Engineered Myoglobins through a One-Electron Reduction Cycle.Journal of the American Chemical Society · 2018Article
- Spectroscopy and DFT Calculations of Flavo-Diiron Nitric Oxide Reductase Identify Bridging Structures of NO-Coordinated Diiron Intermediates.ACS catalysis · 2018Article
- Spectroscopy and DFT Calculations of a Flavo-diiron Enzyme Implicate New Diiron Site Structures.Journal of the American Chemical Society · 2017Article
- A Nonheme, High-Spin {FeNO}Journal of the American Chemical Society · 2017Article
- Structure/function correlations over binuclear non-heme iron active sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Flavodiiron proteins (FDPs) catalyze reductive scavenging of dioxygen and nitric oxide in air-sensitive microorganisms. FDPs contain a distinctive non-heme diiron/flavin mononucleotide (FMN) active site. Alternative mechanisms for the nitric oxide reductase (NOR) activity consisting of either protonation of a diiron-bridging hyponitrite or "super-reduction" of a diferrous-dinitrosyl by the proximal FMNH(2) in the rate-determining step have been proposed. To test these alternative mechanisms, we examined a deflavinated FDP (deflavo-FDP) from Thermotoga maritima. The deflavo-FDP retains an intact diiron site but does not exhibit multiturnover NOR or O(2) reductase (O(2)R) activity. Reactions of the reduced (diferrous) deflavo-FDP with nitric oxide were examined by UV-vis absorption, EPR, resonance Raman, and FTIR spectroscopies. Anaerobic addition of nitric oxide up to one NO per diferrous deflavo-FDP results in formation of a diiron-mononitrosyl complex characterized by a broad S = (1)/(2 )EPR signal arising from antiferromagnetic coupling of an S = (3)/(2) {FeNO}(7) with an S = 2 Fe(II). Further addition of NO results in two reaction pathways, one of which produces N(2)O and the diferric site and the other of which produces a stable diiron-dinitrosyl complex. Both NO-treated and as-isolated deflavo-FDPs regain full NOR and O(2)R activities upon simple addition of FMN. The production of N(2)O upon addition of NO to the mononitrosyl deflavo-FDP supports the hyponitrite mechanism, but the concomitant formation of a stable diiron-dinitrosyl complex in the deflavo-FDP is consistent with a super-reduction pathway in the flavinated enzyme. We conclude that a diiron-mononitrosyl complex is an intermediate in the NOR catalytic cycle of FDPs.
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