Interactions of oxaloacetate with Escherichia coli fumarate reductase☆
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Modular structure of complex II: An evolutionary perspective
2023, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :Besides eukaryotes, these complexes are mainly present in Proteobacteria (Alphaproteobacteria, Betaproteobacteria, and Gammaproteobacteria) being also found within 20 % of unclassified bacterial genomes. Type D, to which E. coli FRD belongs [20,24,47,104–106], has a restricted taxonomic distribution when compared to type A or B. In Bacteria, with exception of Gammaproteobacteria where it is present in 30 % of 5777 metagenomic assemblies, type D is scarcely found across 17 phyla, such as Actinobacteria, Acidobacteria, Calditrichaeota, Bacteroidetes, Candidatus Marinimicrobia, Gemmatimonadetes, and Nitrospirae.
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2012, Journal of Biological ChemistryCitation Excerpt :These dicarboxylates can be either normal metabolic intermediates (18, 19, 29) or toxins (30). For example, fumarate, malate, oxaloacetate, and citrate are all Krebs cycle intermediates with a broad range of Ki values that may regulate complex II activity through feedback inhibition (18, 19). Each of these small molecules has been evaluated to determine the influence on the activity of the E. coli complex II homologs, and all act as either competitive or suicide inhibitors.
Geometric restraint drives on- and off-pathway catalysis by the Escherichia coli menaquinol:fumarate reductase
2011, Journal of Biological ChemistryCitation Excerpt :For example, oxaloacetate is a Krebs cycle intermediate and acts as a tight, slow binding inhibitor of complex II, possibly as a regulatory mechanism (2, 3). It has additionally been proposed that oxaloacetate can be formed through off-pathway catalysis by complex II when fumarate hydration to malate is followed by oxidation to oxaloacetate (3, 4). Oxaloacetate binding to the complex II active site results in a charge transfer complex between the oxaloacetate carbonyl and the FAD hydride that can be monitored spectroscopically (4, 5).
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This work was supported by National Institutes of Health Grant HL-16251, the Veterans Administration, and National Science Foundation Grant DMB-87-15560.