TY - JOUR
T1 - [NiFe], [FeFe], and [Fe] hydrogenase models from isomers
AU - Ogo, Seiji
AU - Kishima, Takahiro
AU - Yatabe, Takeshi
AU - Miyazawa, Keishi
AU - Yamasaki, Ryunosuke
AU - Matsumoto, Takahiro
AU - Ando, Tatsuya
AU - Kikkawa, Mitsuhiro
AU - Isegawa, Miho
AU - Yoon, Ki Seok
AU - Hayami, Shinya
PY - 2020/6
Y1 - 2020/6
N2 - 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.
AB - 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.
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U2 - 10.1126/sciadv.aaz8181
DO - 10.1126/sciadv.aaz8181
M3 - Article
C2 - 32577514
AN - SCOPUS:85086498092
VL - 6
JO - Science advances
JF - Science advances
SN - 2375-2548
IS - 24
M1 - eaaz8181
ER -