ArticleProceedings of the National Academy of Sciences of the United States of America2016
One-carbon chemistry of oxalate oxidoreductase captured by X-ray 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. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Accumulation of heavy metals in the mycelium of Abortiporus biennis and their effect on oxalate oxidase activity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Article
- Effect of alkali metal cations on dehydrogenative coupling of formate anions to oxalate.Frontiers in chemistry · 2025Article
- Structural organization of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina acetivorans.Structure (London, England : 1993) · 2024Article
- Role of oxalic acid in fungal and bacterial metabolism and its biotechnological potential.World journal of microbiology & biotechnology · 2024Review
- Oxalic acid degradation in wood-rotting fungi. Searching for a new source of oxalate oxidase.World journal of microbiology & biotechnology · 2022Article
- X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate.The Journal of biological chemistry · 2019Article
- Article
- Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Properties of Intermediates in the Catalytic Cycle of Oxalate Oxidoreductase and Its Suicide Inactivation by Pyruvate.Biochemistry · 2017Article
- A structural phylogeny for understanding 2-oxoacid oxidoreductase function.Current opinion in structural biology · 2016Review
- Crystal structures of archaeal 2-oxoacid:ferredoxin oxidoreductases from Sulfolobus tokodaii.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Thiamine pyrophosphate (TPP)-dependent oxalate oxidoreductase (OOR) metabolizes oxalate, generating two molecules of CO2 and two low-potential electrons, thus providing both the carbon and reducing equivalents for operation of the Wood-Ljungdahl pathway of acetogenesis. Here we present structures of OOR in which two different reaction intermediate bound states have been trapped: the covalent adducts between TPP and oxalate and between TPP and CO2. These structures, along with the previously determined structure of substrate-free OOR, allow us to visualize how active site rearrangements can drive catalysis. Our results suggest that OOR operates via a bait-and-switch mechanism, attracting substrate into the active site through the presence of positively charged and polar residues, and then altering the electrostatic environment through loop and side chain movements to drive catalysis. This simple but elegant mechanism explains how oxalate, a molecule that humans and most animals cannot break down, can be used for growth by acetogenic bacteria.
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