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Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase

Author(s)
Kim, Sunghwan; Kim, Chang Min; Son, Young-Jin; Choi, Jae Young; Siegenthaler, Rahel K.; Lee, Younho; Jang, Tae-Ho; Song, Jaeyoung; Kang, Hara; Kaiser, Chris A.; Park, Hyun Ho; ... Show more Show less
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Creative Commons Attribution 4.0 International license https://creativecommons.org/licenses/by/4.0/
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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. Keywords: Enzyme mechanisms; Oxidoreductases; X-ray crystallography
Date issued
2018-11
URI
https://hdl.handle.net/1721.1/125140
Department
Massachusetts Institute of Technology. Department of Biology
Journal
Nature Communications
Publisher
Springer Science and Business Media LLC
Citation
Kim, Sunghwan et al. "Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase." Nature Communications 9 (November 2018): 4867 © 2018, The Author(s).
Version: Final published version
ISSN
2041-1723

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