論文

査読有り 国際誌
2020年6月

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

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

6
24
開始ページ
eaaz8181
終了ページ
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1126/sciadv.aaz8181

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.

リンク情報
DOI
https://doi.org/10.1126/sciadv.aaz8181
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32577514
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7286669

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