Journal
SCIENCE
Volume 357, Issue 6354, Pages 928-931Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan4497
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Funding
- Japan Science and Technology Agency CREST, Japan [JPMJCR12M4]
- Japan Society for the Promotion of Science [JP25291038]
- Challenging Exploratory Research [JP24657077]
- Scientific Research on Innovative Areas [JP15H00945]
- Specially Promoted Research [26000008]
- Young Scientists B [JP16K17936]
- Mitsubishi Foundation
- ENEOS Hydrogen Trust Fund
- Platform for Drug Discovery, Informatics, and Structural Life Science) from the Japan Agency for Medical Research and Development (AMED) [1243]
- Academia Sinica
- National Synchrotron Radiation Research Center (Taiwan, ROC)
- Grants-in-Aid for Scientific Research [26000008, 15K05566, 16K17936] Funding Source: KAKEN
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NAD(+) (oxidized form of NAD: nicotinamide adenine dinucleotide)-reducing soluble [ NiFe]hydrogenase (SH) is phylogenetically related to NADH (reduced form of NAD(+)): quinone oxidoreductase (complex I), but the geometrical arrangements of the subunits and Fe-S clusters are unclear. Here, we describe the crystal structures of SH in the oxidized and reduced states. The cluster arrangement is similar to that of complex I, but the subunits orientation is not, which supports the hypothesis that subunits evolved as prebuilt modules. The oxidized active site includes a six-coordinate Ni, which is unprecedented for hydrogenases, whose coordination geometry would prevent O-2 from approaching. In the reduced state showing the normal active site structure without a physiological electron acceptor, the flavin mononucleotide cofactor is dissociated, which may be caused by the oxidation state change of nearby Fe-S clusters and may suppress production of reactive oxygen species.
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