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

July 9, 2020

Title

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

Author

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

Year

2020

Journal

Science Advances

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 H− transfer. 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.

Instrument

V-670

Keywords

Absorption, Quantitation, Inorganic chemistry