ArticleThe Journal of biological chemistry2009
Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 57 citations in OpenAlex.
- Accurate atomic resolution XFEL structures of a metalloenzyme reveal key insights into its catalytic mechanism.Nature communications · 2026Article
- The Long-Range High-pH Proton Channel Facilitates the Nitrite Reduction in Copper-Containing Nitrite Reductase.ACS omega · 2025Article
- Photocatalytic Nitrate Reduction to Ammonia via Zr-Mediated Proton-Coupled Electron Transfer.ChemSusChem · 2025Article
- Discussing the Terms Biomimetic and Bioinspired within Bioinorganic Chemistry.Inorganic chemistry · 2024Article
- Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.The journal of physical chemistry letters · 2022Article
- Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Copper nitrite reductase from Sinorhizobium meliloti 2011: Crystal structure and interaction with the physiological versus a nonmetabolically related cupredoxin-like mediator.Protein science : a publication of the Protein Society · 2021Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Light-Activated Electron Transfer and Catalytic Mechanism of Carnitine Oxidation by Rieske-Type Oxygenase from Human Microbiota.Angewandte Chemie (International ed. in English) · 2021Article
- An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.Science advances · 2021Article
- Active Intermediates in Copper Nitrite Reductase Reactions Probed by a Cryotrapping-Electron Paramagnetic Resonance Approach.Angewandte Chemie (International ed. in English) · 2020Article
- High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.ACS catalysis · 2019Article
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- A QM/MM Study of Nitrite Binding Modes in a Three-Domain Heme-Cu Nitrite Reductase.Molecules (Basel, Switzerland) · 2018Article
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- Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.IUCrJ · 2018Article
- Serial femtosecond crystallography at the SACLA: breakthrough to dynamic structural biology.Biophysical reviews · 2018Review
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The reduction of nitrite (NO2-) into nitric oxide (NO), catalyzed by nitrite reductase, is an important reaction in the denitrification pathway. In this study, the catalytic mechanism of the copper-containing nitrite reductase from Alcaligenes xylosoxidans (AxNiR) has been studied using single and multiple turnover experiments at pH 7.0 and is shown to involve two protons. A novel steady-state assay was developed, in which deoxyhemoglobin was employed as an NO scavenger. A moderate solvent kinetic isotope effect (SKIE) of 1.3 +/- 0.1 indicated the involvement of one protonation to the rate-limiting catalytic step. Laser photoexcitation experiments have been used to obtain single turnover data in H2O and D2O, which report on steps kinetically linked to inter-copper electron transfer (ET). In the absence of nitrite, a normal SKIE of approximately 1.33 +/- 0.05 was obtained, suggesting a protonation event that is kinetically linked to ET in substrate-free AxNiR. A nitrite titration gave a normal hyperbolic behavior for the deuterated sample. However, in H2O an unusual decrease in rate was observed at low nitrite concentrations followed by a subsequent acceleration in rate at nitrite concentrations of >10 mM. As a consequence, the observed ET process was faster in D2O than in H2O above 0.1 mM nitrite, resulting in an inverted SKIE, which featured a significant dependence on the substrate concentration with a minimum value of approximately 0.61 +/- 0.02 between 3 and 10 mM. Our work provides the first experimental demonstration of proton-coupled electron transfer in both the resting and substrate-bound AxNiR, and two protons were found to be involved in turnover.
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