Model compound met the key structural and spectroscopic features of [FeFe]-hydrogenase active site

  1. Li Hai,
  2. Tianyong Zhang,
  3. Shuang Jiang,
  4. Xiaoyuan Ma,
  5. Di Wang and
  6. Bin LiORCID Logo

Submitting author affiliation: Tianjin University, Tianjin, China

Beilstein Arch. 2019, 2019136. doi:10.3762/bxiv.2019.136.v1

Published 30 Oct 2019

  • Preprint

Abstract

Biomimetic synthesis of the [FeFe]-hydrogenase active site draws considerable attention of scientists for its amazing catalytic efficiency on reversible transition between proton and hydrogen. Fe2(CO)3[μ-(SCH(CH2CH3)CH2S)](μ-DPPM)(κ1-DPPM) (compound 1) which replicated key structural aspects of the natural [FeFe]-hydrogenase was designed and synthesized. 1 showed that the wavenumbers in IR were close to those of the natural [FeFe]-hydrogenase active site. In addition, 1 achieved the low oxidation potentials at -0.48 V and -0.26 V, respectively. In the assistance of ethyl located in the S-S bridging structure, the asymmetrical substitution with sterically encumbering and electron-rich ligands in 1 may offer a thorough protection for forming and stabilizing the open site in the rotated structure.

Keywords: [FeFe]-hydrogenase; Structure simulation; Model compound; Enzymes; Oxidation potential

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When a peer-reviewed version of this preprint is available in the Beilstein Journals, this information will be updated in the information box above. If no peer-reviewed version is available, please cite this preprint using the following information:

Hai, L.; Zhang, T.; Jiang, S.; Ma, X.; Wang, D.; Li, B. Beilstein Arch. 2019, 2019136. doi:10.3762/bxiv.2019.136.v1

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