ArticleThe Journal of biological chemistry2011
Geometric restraint drives on- and off-pathway catalysis by the Escherichia coli menaquinol:fumarate reductase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- In Silico Drug Repurposing Endorse Amprenavir, Darunavir and Saquinavir to Target Enzymes of Multidrug Resistant UropathogenicIndian journal of microbiology · 2024Article
- Crystallographic investigation of the ubiquinone binding site of respiratory Complex II and its inhibitors.Biochimica et biophysica acta. Proteins and proteomics · 2021Article
- The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Maturation of the respiratory complex II flavoprotein.Current opinion in structural biology · 2019Review
- New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement.Journal of structural biology · 2018Article
- Crystal structure of an assembly intermediate of respiratory Complex II.Nature communications · 2018Article
- Structural and biochemical analyses reveal insights into covalent flavinylation of theThe Journal of biological chemistry · 2017Article
- Fatty acid nitroalkenes induce resistance to ischemic cardiac injury by modulating mitochondrial respiration at complex II.Redox biology · 2016Article
- Redox state of flavin adenine dinucleotide drives substrate binding and product release in Escherichia coli succinate dehydrogenase.Biochemistry · 2015Article
- Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase.The Journal of biological chemistry · 2013Article
- Catalytic mechanisms of complex II enzymes: a structural perspective.Biochimica et biophysica acta · 2013Review
- Structural basis for malfunction in complex II.The Journal of biological chemistry · 2012Review
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Authors and funding
14 authors at 5 institutions in 2 countries.
Funding
Abstract
Complex II superfamily members catalyze the kinetically difficult interconversion of succinate and fumarate. Due to the relative simplicity of complex II substrates and their similarity to other biologically abundant small molecules, substrate specificity presents a challenge in this system. In order to identify determinants for on-pathway catalysis, off-pathway catalysis, and enzyme inhibition, crystal structures of Escherichia coli menaquinol:fumarate reductase (QFR), a complex II superfamily member, were determined bound to the substrate, fumarate, and the inhibitors oxaloacetate, glutarate, and 3-nitropropionate. Optical difference spectroscopy and computational modeling support a model where QFR twists the dicarboxylate, activating it for catalysis. Orientation of the C2-C3 double bond of activated fumarate parallel to the C(4a)-N5 bond of FAD allows orbital overlap between the substrate and the cofactor, priming the substrate for nucleophilic attack. Off-pathway catalysis, such as the conversion of malate to oxaloacetate or the activation of the toxin 3-nitropropionate may occur when inhibitors bind with a similarly activated bond in the same position. Conversely, inhibitors that do not orient an activatable bond in this manner, such as glutarate and citrate, are excluded from catalysis and act as inhibitors of substrate binding. These results support a model where electronic interactions via geometric constraint and orbital steering underlie catalysis by QFR.
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