ArticleProceedings of the National Academy of Sciences of the United States of America1996
Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 176 citations in OpenAlex.
- First report of neonatal-onset glutaric aciduria type II in the Iranian population caused by a novel deleterious ETFA variant.Orphanet journal of rare diseases · 2025Article
- Unveiling the molecular basis of paracetamol-induced hepatotoxicity: Interaction ofBiochemistry and biophysics reports · 2024Article
- A single hydrogen bond that tunes flavin redox reactivity and activates it for modification.Chemical science · 2024Article
- Quantitative measurements of reactive oxygen species partitioning in electron transfer flavoenzyme magnetic field sensing.Frontiers in physiology · 2024Article
- Characterization of the Membrane-Associated Electron-Bifurcating Flavoenzyme EtfABCX from the Hyperthermophilic BacteriumBiochemistry · 2023Article
- Unusual reactivity of a flavin in a bifurcating electron-transferring flavoprotein leads to flavin modification and a charge-transfer complex.The Journal of biological chemistry · 2022Article
- orsai, the Drosophila homolog of human ETFRF1, links lipid catabolism to growth control.BMC biology · 2022Article
- Long-Time Oxygen Localization in Electron Transfer Flavoprotein.Journal of chemical information and modeling · 2022Article
- Article
- Multi-omics reveals mitochondrial metabolism proteins susceptible for drug discovery in AML.Leukemia · 2022Article
- Contrasting roles for two conserved arginines: Stabilizing flavin semiquinone or quaternary structure, in bifurcating electron transfer flavoproteins.The Journal of biological chemistry · 2022Article
- The role of the electron-transfer flavoprotein: ubiquinone oxidoreductase following carbohydrate starvation in Arabidopsis cell cultures.Plant cell reports · 2022Article
- Nitrogen nutrition contributes to plant fertility by affecting meiosis initiation.Nature communications · 2022Article
- Diagnostic Challenges in Late Onset Multiple Acyl-CoA Dehydrogenase Deficiency: Clinical, Morphological, and Genetic Aspects.Frontiers in neurology · 2022Article
- Multiple acyl-CoA dehydrogenase deficiency kills Mycobacterium tuberculosis in vitro and during infection.Nature communications · 2021Article
- Allele-specific assembly of a eukaryotic genome corrects apparent frameshifts and reveals a lack of nonsense-mediated mRNA decay.NAR genomics and bioinformatics · 2021Article
- Article
- Use of MALDI Mass Spectrometry Imaging to Identify Proteomic Signatures in Aortic Aneurysms after Endovascular Repair.Biomedicines · 2021Article
- Review
- Cryoelectron microscopy structure and mechanism of the membrane-associated electron-bifurcating flavoprotein Fix/EtfABCX.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mammalian electron transfer flavoproteins (ETF) are heterodimers containing a single equivalent of flavin adenine dinucleotide (FAD). They function as electron shuttles between primary flavoprotein dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. The structure of human ETF solved to 2.1-A resolution reveals that the ETF molecule is comprised of three distinct domains: two domains are contributed by the alpha subunit and the third domain is made up entirely by the beta subunit. The N-terminal portion of the alpha subunit and the majority of the beta subunit have identical polypeptide folds, in the absence of any sequence homology. FAD lies in a cleft between the two subunits, with most of the FAD molecule residing in the C-terminal portion of the alpha subunit. Alignment of all the known sequences for the ETF alpha subunits together with the putative FixB gene product shows that the residues directly involved in FAD binding are conserved. A hydrogen bond is formed between the N5 of the FAD isoalloxazine ring and the hydroxyl side chain of alpha T266, suggesting why the pathogenic mutation, alpha T266M, affects ETF activity in patients with glutaric acidemia type II. Hydrogen bonds between the 4'-hydroxyl of the ribityl chain of FAD and N1 of the isoalloxazine ring, and between alpha H286 and the C2-carbonyl oxygen of the isoalloxazine ring, may play a role in the stabilization of the anionic semiquinone. With the known structure of medium chain acyl-CoA dehydrogenase, we hypothesize a possible structure for docking the two proteins.
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