TY - JOUR
T1 - Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase
AU - Muraki, Norifumi
AU - Ishii, Kentaro
AU - Uchiyama, Susumu
AU - Itoh, Satoru G.
AU - Okumura, Hisashi
AU - Aono, Shigetoshi
N1 - Funding Information:
We thank Nicolas Moghaddam, who was an international internship trainee from Chimie Paris Tech in Institute for Molecular Science, for his effort on screening of purification and crystallization conditions for HypX at the preliminary stage of this work. This work was performed using a synchrotron beamline BL44XU at SPring-8 under the Collaborative Research Program of Institute for Protein Research, Osaka University. Diffraction data were collected at the Osaka University beamline BL44XU at SPring-8 (Harima, Japan) (Proposal No. 2017A6757, 2017B6757, 2018A6853, and 2018B6853). We thank Dr. Eiki Yamashita, Dr. Akifumi Higashiura, and Dr. Kenji Takagi for their help during data collection. The MD simulations were performed using Research Center for Computational Science, Okazaki Research Facilities, National Institutes of Natural Sciences. This work was supported by a Grant-in-Aid for Scientific Research (B) 17H03093 to S.A and Joint Research by Exploratory Research Center on Life and Living Systems (ExCELLS).
Publisher Copyright:
© 2019, The Author(s).
PY - 2019/12/1
Y1 - 2019/12/1
N2 - Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN− are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N10-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct experimental results are not available yet. The conformation of CoA accommodated in the continuous cavity connecting the N- and C-terminal domains will interconvert between the extended and the folded conformations for HypX catalysis.
AB - Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN− are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N10-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct experimental results are not available yet. The conformation of CoA accommodated in the continuous cavity connecting the N- and C-terminal domains will interconvert between the extended and the folded conformations for HypX catalysis.
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U2 - 10.1038/s42003-019-0631-z
DO - 10.1038/s42003-019-0631-z
M3 - Article
C2 - 31646188
AN - SCOPUS:85073561448
SN - 2399-3642
VL - 2
JO - Communications biology
JF - Communications biology
IS - 1
M1 - 385
ER -