ArticleThe Journal of biological chemistry2016
Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways.International journal of molecular sciences · 2020Review
- Extracellular electron transfer powers flavinylated extracellular reductases in Gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Maturation of the respiratory complex II flavoprotein.Current opinion in structural biology · 2019Review
- The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.Cellular and molecular life sciences : CMLS · 2019Review
- 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
- Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE.Proceedings of the National Academy of Sciences of the United States of America · 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
- SLC25 Family Member Genetic Interactions Identify a Role forG3 (Bethesda, Md.) · 2017Article
- The Assembly Factor SDHAF2 Is Dispensable for Flavination of the Catalytic Subunit of Mitochondrial Complex II in Breast Cancer Cells.The Journal of biological chemistry · 2016Article
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Authors and funding
8 authors.
Funding
Abstract
Escherichia coli harbors two highly conserved homologs of the essential mitochondrial respiratory complex II (succinate:ubiquinone oxidoreductase). Aerobically the bacterium synthesizes succinate:quinone reductase as part of its respiratory chain, whereas under microaerophilic conditions, the quinol:fumarate reductase can be utilized. All complex II enzymes harbor a covalently bound FAD co-factor that is essential for their ability to oxidize succinate. In eukaryotes and many bacteria, assembly of the covalent flavin linkage is facilitated by a small protein assembly factor, termed SdhE in E. coli. How SdhE assists with formation of the covalent flavin bond and how it binds the flavoprotein subunit of complex II remain unknown. Using photo-cross-linking, we report the interaction site between the flavoprotein of complex II and the SdhE assembly factor. These data indicate that SdhE binds to the flavoprotein between two independently folded domains and that this binding mode likely influences the interdomain orientation. In so doing, SdhE likely orients amino acid residues near the dicarboxylate and FAD binding site, which facilitates formation of the covalent flavin linkage. These studies identify how the conserved SdhE assembly factor and its homologs participate in complex II maturation.
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