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

Sunghwan Kim (), Chang Min Kim, Young-Jin Son, Jae Young Choi, Rahel K. Siegenthaler, Younho Lee, Tae-Ho Jang, Jaeyoung Song, Hara Kang, Chris A. Kaiser and Hyun Ho Park ()
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Sunghwan Kim: Daegu-Gyeongbuk Medical Innovation Foundation
Chang Min Kim: Chung-Ang University
Young-Jin Son: Daegu-Gyeongbuk Medical Innovation Foundation
Jae Young Choi: Yeungnam University
Rahel K. Siegenthaler: Massachusetts Institute of Technology
Younho Lee: Yonsei University
Tae-Ho Jang: Daegu-Gyeongbuk Medical Innovation Foundation
Jaeyoung Song: Daegu-Gyeongbuk Medical Innovation Foundation
Hara Kang: Incheon National University
Chris A. Kaiser: Massachusetts Institute of Technology
Hyun Ho Park: Chung-Ang University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-07285-9

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