[NiFe], [FeFe], and [Fe] hydrogenase models from isomers

Seiji Ogo, Takahiro Kishima, Takeshi Yatabe, Keishi Miyazawa, Ryunosuke Yamasaki, Takahiro Matsumoto, Tatsuya Ando, Mitsuhiro Kikkawa, Miho Isegawa, Ki Seok Yoon, Shinya Hayami

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Abstract

The study of hydrogenase enzymes (H2ases) is necessary because of their importance to a future hydrogen energy economy. These enzymes come in three distinct classes: [NiFe] H2ases, which have a propensity toward H2 oxidation; [FeFe] H2ases, which have a propensity toward H2 evolution; and [Fe] H2ases, which catalyze Htransfer. Modeling these enzymes has so far treated them as different species, which is understandable given the different cores and ligand sets of the natural molecules. Here, we demonstrate, using x-ray analysis and nuclear magnetic resonance, infrared, Mössbauer spectroscopies, and electrochemical measurement, that the catalytic properties of all three enzymes can be mimicked with only three isomers of the same NiFe complex.

Original languageEnglish
Article numbereaaz8181
JournalScience Advances
Volume6
Issue number24
DOIs
Publication statusPublished - Jun 2020

All Science Journal Classification (ASJC) codes

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    Ogo, S., Kishima, T., Yatabe, T., Miyazawa, K., Yamasaki, R., Matsumoto, T., Ando, T., Kikkawa, M., Isegawa, M., Yoon, K. S., & Hayami, S. (2020). [NiFe], [FeFe], and [Fe] hydrogenase models from isomers. Science Advances, 6(24), [eaaz8181]. https://doi.org/10.1126/sciadv.aaz8181