ArticleScientific reports2017
The active site structure and catalytic mechanism of arsenite oxidase.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The key to arsenic pollution remediation: engineering and functional effects of arsenic-resistant microorganisms.World journal of microbiology & biotechnology · 2026Review
- Active Site Characterization of aInorganic chemistry · 2024Article
- Bacterial biota associated with the invasive insect pest Tuta absoluta (Meyrick).Scientific reports · 2024Article
- Spectroscopic and Structural Characterization of ReducedACS chemical biology · 2022Article
- Different Regulatory Strategies of Arsenite Oxidation by Two IsolatedFrontiers in microbiology · 2022Article
- Article
- Methane, arsenic, selenium and the origins of the DMSO reductase family.Scientific reports · 2020Article
- Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Microbial Oxidation of Arsenite: Regulation, Chemotaxis, Phosphate Metabolism and Energy Generation.Frontiers in microbiology · 2020Review
- Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str. NT-26 using a combination of X-ray absorption spectroscopy and computational chemistry. Our analysis indicates an oxidized Mo(VI) active site with a structure that is far from equilibrium. We propose that this is an entatic state imposed by the protein on the active site through relative orientation of the two molybdopterin cofactors, in a variant of the Rây-Dutt twist of classical coordination chemistry, which we call the pterin twist hypothesis. We discuss the implications of this hypothesis for other putatively ancient molybdopterin-based enzymes.
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