ArticleChemical science2020
Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Accurate atomic resolution XFEL structures of a metalloenzyme reveal key insights into its catalytic mechanism.Nature communications · 2026Article
- Coupled on-line in crystallo UV-Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature.Acta crystallographica. Section D, Structural biology · 2026Article
- 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
- An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.Science advances · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The design and synthesis of copper complexes that can reduce nitrite to NO has attracted considerable interest. They have been guided by the structural information on the catalytic Cu centre of the widespread enzymes Cu nitrite reductases but the chemically novel side-on binding of NO observed in all crystallographic studies of these enzymes has been questioned in terms of its functional relevance. We show conversion of NO
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