ArticleProceedings of the National Academy of Sciences of the United States of America2016
Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.
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46 citing papers in PubMed, 104 citations in OpenAlex.
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- The Long-Range High-pH Proton Channel Facilitates the Nitrite Reduction in Copper-Containing Nitrite Reductase.ACS omega · 2025Article
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- Lewis acid-assisted reduction of nitrite to nitric and nitrous oxides via the elusive nitrite radical dianion.Nature chemistry · 2022Article
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- 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
- Involvement of a Formally Copper(III) Nitrite Complex in Proton-Coupled Electron Transfer and Nitration of Phenols.Inorganic chemistry · 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
- Mechanism of O-Atom Transfer from Nitrite: Nitric Oxide Release at Copper(II).Inorganic chemistry · 2021Article
- Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins.Membranes · 2021Review
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Synchrotron Radiation as a Tool for Macromolecular X-Ray Crystallography: a XXI Century Perspective.Nuclear instruments & methods in physics research. Section B, Beam interactions with materials and atoms · 2021Article
- An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.Science advances · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
22 authors at 10 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proton-coupled electron transfer (PCET), a ubiquitous phenomenon in biological systems, plays an essential role in copper nitrite reductase (CuNiR), the key metalloenzyme in microbial denitrification of the global nitrogen cycle. Analyses of the nitrite reduction mechanism in CuNiR with conventional synchrotron radiation crystallography (SRX) have been faced with difficulties, because X-ray photoreduction changes the native structures of metal centers and the enzyme-substrate complex. Using serial femtosecond crystallography (SFX), we determined the intact structures of CuNiR in the resting state and the nitrite complex (NC) state at 2.03- and 1.60-Å resolution, respectively. Furthermore, the SRX NC structure representing a transient state in the catalytic cycle was determined at 1.30-Å resolution. Comparison between SRX and SFX structures revealed that photoreduction changes the coordination manner of the substrate and that catalytically important His255 can switch hydrogen bond partners between the backbone carbonyl oxygen of nearby Glu279 and the side-chain hydroxyl group of Thr280. These findings, which SRX has failed to uncover, propose a redox-coupled proton switch for PCET. This concept can explain how proton transfer to the substrate is involved in intramolecular electron transfer and why substrate binding accelerates PCET. Our study demonstrates the potential of SFX as a powerful tool to study redox processes in metalloenzymes.
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