Communication

Reversible Protonation of a Thiolate Ligand in an [Fe]-Hydrogenase Model Complex†

  1. Dr. Dafa Chen,
  2. Dr. Rosario Scopelliti,
  3. Prof. Dr. Xile Hu*

Article first published online: 10 JAN 2012

DOI: 10.1002/anie.201107634

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 51, Issue 8, pages 1919–1921, February 20, 2012

Additional Information

How to Cite

Chen, D., Scopelliti, R. and Hu, X. (2012), Reversible Protonation of a Thiolate Ligand in an [Fe]-Hydrogenase Model Complex. Angew. Chem. Int. Ed., 51: 1919–1921. doi: 10.1002/anie.201107634

Author Information

  1. Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), ISIC-LSCI, BCH 3305, Lausanne 1015 (Switzerland) http://lsci.epfl.ch

*Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), ISIC-LSCI, BCH 3305, Lausanne 1015 (Switzerland) http://lsci.epfl.ch

  1. †

    This work is supported by the Swiss National Science Foundation (project no. 200020_134473/1).

Publication History

  1. Issue published online: 14 FEB 2012
  2. Article first published online: 10 JAN 2012
  3. Manuscript Received: 29 OCT 2011

Funded by

  • Swiss National Science Foundation. Grant Number: 200020_134473/1

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

View Full Article with Supporting Information (HTML) Get PDF (395K)

Keywords:

  • enzyme models;
  • hydrogenases;
  • iron;
  • protonation;
  • sulfur
Thumbnail image of graphical abstract

What is the channel? The thiolate ligand in the five-coordinate model complex 1 of [Fe]-hydrogenase is preferentially and reversibly protonated, even in the presence of an acyl ligand. The results suggest that the Cys176 thiolate ligand in [Fe]-hydrogenase can serve as the internal base to accept the proton after heterolytic splitting of H2.

View Full Article with Supporting Information (HTML) Get PDF (395K)