ArticleBiochemistry2014
A diferrous-dinitrosyl intermediate in the N2O-generating pathway of a deflavinated flavo-diiron protein.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 43 citations in OpenAlex.
- The Role of Iron-Hyponitrite Intermediates in Biology and Insights From Synthetic Model Complexes.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Synthesis and Structural Characterization of a Non-Heme Iron Hyponitrite Complex.Angewandte Chemie (International ed. in English) · 2024Article
- Particle Swarm Fitting of Spin Hamiltonians: Magnetic Circular Dichroism of Reduced and NO-Bound Flavodiiron Protein.Inorganic chemistry · 2022Article
- 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
- 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
- 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
- The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
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5 authors at 2 institutions in 1 country.
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Abstract
Flavo-diiron proteins (FDPs) function as anaerobic nitric oxide scavengers in some microorganisms, catalyzing reduction of nitric to nitrous oxide. The FDP from Thermotoga maritima can be prepared in a deflavinated form with an intact diferric site (deflavo-FDP). Hayashi et al. [(2010) Biochemistry 49, 7040-7049] reported that reaction of NO with reduced deflavo-FDP produced substoichiometric N2O. Here we report a multispectroscopic approach to identify the iron species in the reactions of deflavo-FDP with NO. Mössbauer spectroscopy identified two distinct ferrous species after reduction of the antiferromagnetically coupled diferric site. Approximately 60% of the total ferrous iron was assigned to a diferrous species associated with the N2O-generating pathway. This pathway proceeds through successive diferrous-mononitrosyl (S = (1)/2 Fe(II){FeNO}(7)) and diferrous-dinitrosyl (S = 0 [{FeNO}(7)]2) species that form within ∼100 ms of mixing of the reduced protein with NO. The diferrous-dinitrosyl intermediate converted to an antiferromagnetically coupled diferric species that was spectroscopically indistinguishable from that in the starting deflavinated protein. These diiron species closely resembled those reported for the flavinated FDP [Caranto et al. (2014) J. Am. Chem. Soc. 136, 7981-7992], and the time scales of their formation and decay were consistent with the steady state turnover of the flavinated protein. The remaining ∼40% of ferrous iron was inactive in N2O generation but reversibly bound NO to give an S = (3)/2 {FeNO}(7) species. The results demonstrate that N2O formation in FDPs can occur via conversion of S = 0 [{FeNO}(7)]2 to a diferric form without participation of the flavin cofactor.
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