{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(1)"],"submitter":["Kim S"],"pubmed_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 c"],"journal":["Nature communications"],"pagination":["4867"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6242907"],"repository":["biostudies-literature"],"pubmed_title":["Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase."],"pmcid":["PMC6242907"],"pubmed_authors":["Kim S","Kang H","Jang TH","Choi JY","Park HH","Siegenthaler RK","Lee Y","Kaiser CA","Kim CM","Song J","Son YJ"],"additional_accession":[]},"is_claimable":false,"name":"Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase.","description":"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 c","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Nov","modification":"2026-05-06T06:29:18.779Z","creation":"2019-03-27T00:08:46Z"},"accession":"S-EPMC6242907","cross_references":{"pubmed":["30451826"],"doi":["10.1038/s41467-018-07285-9"]}}