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  4. Reversible protonation of a thiolate ligand in an [Fe]-hydrogenase model complex
 
research article

Reversible protonation of a thiolate ligand in an [Fe]-hydrogenase model complex

Chen, Dafa  
•
Scopelliti, Rosario  
•
Hu, Xile  
2012
Angewandte Chemie International Edition

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.

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Type
research article
DOI
10.1002/anie.201107634
Web of Science ID

WOS:000300446100033

Author(s)
Chen, Dafa  
Scopelliti, Rosario  
Hu, Xile  
Date Issued

2012

Publisher

Wiley-VCH Verlag GmbH

Published in
Angewandte Chemie International Edition
Volume

51

Issue

8

Start page

1919

End page

1921

Subjects

Enzyme models

•

Hydrogenase

•

Iron

•

Protonation

•

Sulfur

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LSCI  
Available on Infoscience
February 15, 2012
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/77760
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