ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2024
Insights into periplasmic nitrate reductase function under single turnover.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Advances in the DMSO reductase family: From discovery to mechanism.Current opinion in chemical biology · 2026Review
- Structure and function of periplasmic nitrate reductase.Biochemical Society transactions · 2026Review
- Ecological Imprint of Rare Earth Mining on Microbial Communities and Water Quality Across Depth and Distance Gradients in Ganzhou, China.Microorganisms · 2025Article
- Nitrate-Nitrite Interplay in the Nitrogen Biocycle.Molecules (Basel, Switzerland) · 2025Review
- Reversible Interconversion of Nitrate and Nitrite Catalyzed by Periplasmic Nitrate Reductase fromJournal of the American Chemical Society · 2025Article
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Authors and funding
7 authors.
Funding
Abstract
Nitrate reductases play pivotal roles in nitrogen metabolism by leveraging the molybdopterin cofactor to facilitate the reduction of nitrate to nitrite. Periplasmic nitrate reductases (NapA) utilize nitrate as a terminal electron acceptor when oxygen is limiting, helping to drive anaerobic metabolism in bacteria. Despite extensive research into NapA homologs, open questions about the mechanism remain especially at the molecular level. More broadly, little is understood of how the molybdopterin cofactor is tuned for catalysis in these enzymes enabling broad substrate scope and reactivity observed in molybdenum-containing enzymes. Here, we have prepared NapA from Campylobacter jejuni under single turnover conditions to generate a singly reduced enzyme that can be further examined by electron paramagnetic resonance (EPR) spectroscopy. Our results provide new context into the known spectra and related structures of NapA and related enzymes. These insights open new avenues for understanding nitrate reductase mechanisms, molybdenum coordination dynamics, and the role of pyranopterin ligands in catalysis.
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