TY - JOUR
T1 - Structural basis of the redox switches in the NAD+-reducing soluble [NiFe]-hydrogenase
AU - Shomura, Y.
AU - Taketa, M.
AU - Nakashima, H.
AU - Tai, H.
AU - Nakagawa, H.
AU - Ikeda, Y.
AU - Ishii, M.
AU - Igarashi, Y.
AU - Nishihara, H.
AU - Yoon, K. S.
AU - Ogo, S.
AU - Hirota, S.
AU - Higuchi, Y.
N1 - Funding Information:
This work was supported by Japan Science and Technology Agency CREST grant JPMJCR12M4, Japan (Y.H. and S.H.), Japan Society for the Promotion of Science [Category B, grant JP25291038 (Y.H.); Challenging Exploratory Research, grant JP24657077 (Y.H.); Scientific Research on Innovative Areas, grant JP15H00945 (S.H.); Specially Promoted Research, grant 26000008 (S.O.); and Young Scientists B, grant JP16K17936 (H.T.)], and by research grants from The Mitsubishi Foundation (Y.H.) and ENEOS Hydrogen Trust Fund (Y.H.). We thank M. Habukawa, K. Hataguchi, and K. Matsumoto for their support with enzyme preparation. The synchrotron radiation experiments were performed at the BL38B1 (proposals 21013 and 25476), BL41XU (proposal 22996), BL44XU (proposals 21817, 23301, 24798, and 26479), and BL32XU [Platform Project for Supporting in Drug Discovery and Life Science Research (Platform for Drug Discovery, Informatics, and Structural Life Science) from the Japan Agency for Medical Research and Development (AMED) (project 1243)]. The charge-coupled device detector MX225-HE (Rayonix) at BL44XU was financially supported by Academia Sinica and the National Synchrotron Radiation Research Center (Taiwan, ROC). Coordinates and structure factors for the x-ray crystal structures of SH in the air-oxidized and H2-reduced states have been deposited in the Protein Data Bank (PDB) with accession codes of 5XF9 and 5XFA, respectively.
PY - 2017/9/1
Y1 - 2017/9/1
N2 - 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 O2 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.
AB - 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 O2 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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U2 - 10.1126/science.aan4497
DO - 10.1126/science.aan4497
M3 - Article
C2 - 28860386
AN - SCOPUS:85029514393
VL - 357
SP - 928
EP - 932
JO - Science
JF - Science
SN - 0036-8075
IS - 6354
ER -