ArticleNature communications2018
Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 39 citations in OpenAlex.
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- Reconfiguration of the reductive TCA cycle enables high-level succinic acid production by Yarrowia lipolytica.Nature communications · 2023Article
- An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond.The Journal of biological chemistry · 2023Review
- Endoplasmic reticulum oxidoreductin provides resilience against reductive stress and hypoxic conditions by mediating luminal redox dynamics.The Plant cell · 2022Article
- Imidazole and nitroimidazole derivatives as NADH-fumarate reductase inhibitors: Density functional theory studies, homology modeling, and molecular docking.Journal of computational chemistry · 2022Article
- A Novel, NADH-Dependent Acrylate Reductase in Vibrio harveyi.Applied and environmental microbiology · 2022Article
- Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production.Nature communications · 2021Article
- Mechanisms of Hypercapnia-Induced Endoplasmic Reticulum Dysfunction.Frontiers in physiology · 2021Review
- Review
- 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
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Osm1 and Frd1 are soluble fumarate reductases from yeast that are critical for allowing survival under anaerobic conditions. Although they maintain redox balance during anaerobiosis, the underlying mechanism is not understood. Here, we report the crystal structure of a eukaryotic soluble fumarate reductase, which is unique among soluble fumarate reductases as it lacks a heme domain. Structural and enzymatic analyses indicate that Osm1 has a specific binding pocket for flavin molecules, including FAD, FMN, and riboflavin, catalyzing their oxidation while reducing fumarate to succinate. Moreover, ER-resident Osm1 can transfer electrons from the Ero1 FAD cofactor to fumarate either by free FAD or by a direct interaction, allowing de novo disulfide bond formation in the absence of oxygen. We conclude that soluble eukaryotic fumarate reductases can maintain an oxidizing environment under anaerobic conditions, either by oxidizing cellular flavin cofactors or by a direct interaction with flavoenzymes such as Ero1.
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