ArticleProceedings of the National Academy of Sciences of the United States of America2020
High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 35 citations in OpenAlex.
- Accurate atomic resolution XFEL structures of a metalloenzyme reveal key insights into its catalytic mechanism.Nature communications · 2026Article
- Discussing the Terms Biomimetic and Bioinspired within Bioinorganic Chemistry.Inorganic chemistry · 2024Article
- Role of Protonation States in the Stability of Molecular Dynamics Simulations of High-Resolution Membrane Protein Structures.The journal of physical chemistry. B · 2024Article
- Improved joint X-ray and neutron refinement procedure in Phenix.Acta crystallographica. Section D, Structural biology · 2023Article
- Description of peptide bond planarity from high-resolution neutron crystallography.Biophysics and physicobiology · 2023Article
- Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis.Science advances · 2022Article
- Current status of neutron crystallography in structural biology.Biophysics and physicobiology · 2022Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.Science advances · 2021Article
- Semi-empirical model to estimate ideal conditions for the growth of large protein crystals.Acta crystallographica. Section D, Structural biology · 2020Article
- Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis.Chemical science · 2020Article
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5 authors at 3 institutions in 1 country.
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Abstract
Copper-containing nitrite reductases (CuNIRs) transform nitrite to gaseous nitric oxide, which is a key process in the global nitrogen cycle. The catalytic mechanism has been extensively studied to ultimately achieve rational control of this important geobiochemical reaction. However, accumulated structural biology data show discrepancies with spectroscopic and computational studies; hence, the reaction mechanism is still controversial. In particular, the details of the proton transfer involved in it are largely unknown. This situation arises from the failure of determining positions of hydrogen atoms and protons, which play essential roles at the catalytic site of CuNIRs, even with atomic resolution X-ray crystallography. Here, we determined the 1.50 Å resolution neutron structure of a CuNIR from
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