ArticleBiochemistry2015
The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Indole-3-acetic acid production is rare among gut bacteria and reflects OFOR-driven amino acid oxidation in acetogens.Gut microbes · 2026Article
- Indole-3-acetic acid production is rare among gut bacteria and reflects OFOR-driven amino acid oxidation in acetogens.bioRxiv : the preprint server for biology · 2026Article
- 2-oxoglutarate:acceptor oxidoreductase-catalyzed redox cycling effectively targets coccoid forms of Helicobacter pylori.Nature communications · 2025Article
- Structural organization of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina acetivorans.Structure (London, England : 1993) · 2024Article
- Deficient butyrate metabolism in the intestinal microbiome is a potential risk factor for recurrent kidney stone disease.Urolithiasis · 2024Article
- Insights into Enzyme Reactions with Redox Cofactors in Biological Conversion of COJournal of microbiology and biotechnology · 2023Review
- 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
- Crosstalk between the tricarboxylic acid cycle and peptidoglycan synthesis in Caulobacter crescentus through the homeostatic control of α-ketoglutarate.PLoS genetics · 2017Article
- 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
- One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Thiamine pyrophosphate (TPP), a derivative of vitamin B1, is a versatile and ubiquitous cofactor. When coupled with [4Fe-4S] clusters in microbial 2-oxoacid:ferredoxin oxidoreductases (OFORs), TPP is involved in catalyzing low-potential redox reactions that are important for the synthesis of key metabolites and the reduction of N2, H(+), and CO2. We have determined the high-resolution (2.27 Å) crystal structure of the TPP-dependent oxalate oxidoreductase (OOR), an enzyme that allows microbes to grow on oxalate, a widely occurring dicarboxylic acid that is found in soil and freshwater and is responsible for kidney stone disease in humans. OOR catalyzes the anaerobic oxidation of oxalate, harvesting the low-potential electrons for use in anaerobic reduction and fixation of CO2. We compare the OOR structure to that of the only other structurally characterized OFOR family member, pyruvate:ferredoxin oxidoreductase. This side-by-side structural analysis highlights the key similarities and differences that are relevant for the chemistry of this entire class of TPP-utilizing enzymes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.