ArticleThe Journal of biological chemistry2008
A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Cryo-EM structure of the yeast Saccharomyces cerevisiae SDH provides a template for eco-friendly fungicide discovery.Nature communications · 2025Article
- A Novel Human SDHA-Knockout Cell Line Model for the Functional Analysis of Clinically Relevant SDHA Variants.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024Article
- An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond.The Journal of biological chemistry · 2023Review
- Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster.Proceedings of the National Academy of Sciences of the United States of America · 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
- Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF.Nature communications · 2020Article
- The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS.The Journal of biological chemistry · 2018Article
- 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
- Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II.The Journal of biological chemistry · 2016Article
- Redox state of flavin adenine dinucleotide drives substrate binding and product release in Escherichia coli succinate dehydrogenase.Biochemistry · 2015Article
- Catalytic mechanisms of complex II enzymes: a structural perspective.Biochimica et biophysica acta · 2013Review
- Sequence diversity and conservation in factors influencing succinate dehydrogenase flavinylation.Plant signaling & behavior · 2013Review
- Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit.The Journal of biological chemistry · 2012Article
- Structural basis for malfunction in complex II.The Journal of biological chemistry · 2012Review
- Molecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase.Biochemistry · 2012Article
- Genome-wide characterization of new and drought stress responsive microRNAs in Populus euphratica.Journal of experimental botany · 2011Article
- Geometric restraint drives on- and off-pathway catalysis by the Escherichia coli menaquinol:fumarate reductase.The Journal of biological chemistry · 2011Article
- Succinate dehydrogenase - Assembly, regulation and role in human disease.Mitochondrion · 2010Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
In Escherichia coli, the complex II superfamily members succinate:ubiquinone oxidoreductase (SQR) and quinol:fumarate reductase (QFR) participate in aerobic and anaerobic respiration, respectively. Complex II enzymes catalyze succinate and fumarate interconversion at the interface of two domains of the soluble flavoprotein subunit, the FAD binding domain and the capping domain. An 11-amino acid loop in the capping domain (Thr-A234 to Thr-A244 in quinol:fumarate reductase) begins at the interdomain hinge and covers the active site. Amino acids of this loop interact with both the substrate and a proton shuttle, potentially coordinating substrate binding and the proton shuttle protonation state. To assess the loop's role in catalysis, two threonine residues were mutated to alanine: QFR Thr-A244 (act-T; Thr-A254 in SQR), which hydrogen-bonds to the substrate at the active site, and QFR Thr-A234 (hinge-T; Thr-A244 in SQR), which is located at the hinge and hydrogen-bonds the proton shuttle. Both mutations impair catalysis and decrease substrate binding. The crystal structure of the hinge-T mutation reveals a reorientation between the FAD-binding and capping domains that accompanies proton shuttle alteration. Taken together, hydrogen bonding from act-T to substrate may coordinate with interdomain motions to twist the double bond of fumarate and introduce the strain important for attaining the transition state.
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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.