ArticleNature communications2018
Crystal structure of an assembly intermediate of respiratory Complex II.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- MICU proteins facilitate calcium-dependent mitochondrial metabolon formation to regulate cellular energetics independently of MCU.Nature metabolism · 2026Article
- Review
- Complex II assembly drives metabolic adaptation to OXPHOS dysfunction.Science advances · 2025Article
- Mitochondrial metabolism and cancer therapeutic innovation.Signal transduction and targeted therapy · 2025Review
- MICU proteins facilitate CaResearch square · 2025Article
- An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond.The Journal of biological chemistry · 2023Review
- Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022Review
- YgfY Contributes to Stress Tolerance inMicroorganisms · 2021Article
- 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
- Mitochondrial complex II and reactive oxygen species in disease and therapy.Redox report : communications in free radical research · 2020Review
- 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
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- 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
- A Mechanism of Modulating the Direction of Flagellar Rotation in Bacteria by Fumarate and Fumarate Reductase.Journal of molecular biology · 2019Article
- 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
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Flavin is covalently attached to the protein scaffold in ~10% of flavoenzymes. However, the mechanism of covalent modification is unclear, due in part to challenges in stabilizing assembly intermediates. Here, we capture the structure of an assembly intermediate of the Escherichia coli Complex II (quinol:fumarate reductase (FrdABCD)). The structure contains the E. coli FrdA subunit bound to covalent FAD and crosslinked with its assembly factor, SdhE. The structure contains two global conformational changes as compared to prior structures of the mature protein: the rotation of a domain within the FrdA subunit, and the destabilization of two large loops of the FrdA subunit, which may create a tunnel to the active site. We infer a mechanism for covalent flavinylation. As supported by spectroscopic and kinetic analyses, we suggest that SdhE shifts the conformational equilibrium of the FrdA active site to disfavor succinate/fumarate interconversion and enhance covalent flavinylation.
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