Issue 25, 2014

[NiFe] hydrogenases: how close do structural and functional mimics approach the active site?

Abstract

Hydrogen is being considered as a versatile alternative fuel with the ever increasing energy demand and oil prices. Hydrogenases (H2ases) found in bacteria, archaea and eukaryotes are very efficient catalysts for biological hydrogen production. An important and unique hydrogenase enzyme is the [NiFe] H2ase, with an unusual heterobimetallic site. Since the determination of its crystal structure, a variety of complexes have been synthesised and studied. Bioinspired and biomimetic complexes have been investigated as potential catalysts. So far, of all the reported complexes only a few of them have been found to be catalytically active. Moreover, most of the reports are on the reverse reaction, e.g. proton reduction rather than dihydrogen oxidation. This perspective article therefore reviews the structural and functional aspects of the very recently reported model complexes that mimic the [NiFe] hydrogenase active site either in structure or function or both.

Graphical abstract: [NiFe] hydrogenases: how close do structural and functional mimics approach the active site?

Article information

Article type
Perspective
Submitted
20 Feb 2014
Accepted
20 Mar 2014
First published
20 May 2014
This article is Open Access
Creative Commons BY license

Dalton Trans., 2014,43, 9392-9405

[NiFe] hydrogenases: how close do structural and functional mimics approach the active site?

S. Kaur-Ghumaan and M. Stein, Dalton Trans., 2014, 43, 9392 DOI: 10.1039/C4DT00539B

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