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Journal Article

The atomic-resolution crystal structure of activated [Fe]-hydrogenase

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Huang,  Gangfeng
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Bill,  Eckhard
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Huang, G., Wagner, T., Wodrich, M. D., Ataka, K., Bill, E., Ermler, U., et al. (2019). The atomic-resolution crystal structure of activated [Fe]-hydrogenase. Nature Catalysis, 2(6), 537-543. doi:10.1038/s41929-019-0289-4.


Cite as: https://hdl.handle.net/21.11116/0000-0008-F2E0-9
Abstract
Hydrogenases are promising templates for constructing new H-2-based catalysts. [Fe]-hydrogenase, which features an ironguanylylpyridinol (FeGP) cofactor, catalyses a reversible hydride transfer from H-2 to methenyl-tetrahydromethanopterin (methenyl-H4MPT+, a C-1 carrier in methanogens). Here, we present a detailed mechanistic scenario of this reaction based on the 1.06 angstrom resolution structure of [Fe]-hydrogenase in a closed active form, in which the Fe of the FeGP cofactor is positioned near the hydride-accepting C14a of a remarkably distorted methenyl-H4MPT+. The open-to-closed transition generates an unsaturated pentacoordinated Fe on expulsion of a water ligand. Quantum mechanics/molecular mechanics computations based on experimental models indicate that a deprotonated 2-OH group on the FeGP cofactor acts as a catalytic base and provides a fairly complete picture of H-2 activation: H-2 binding on the empty Fe site was found to be nearly thermo-neutral while H-2 cleavage and hydride transfer proceed smoothly. The overall reaction involves a repositioning and relaxation of the distorted methenyl-H4MPT+.