Jump to main content
Jump to site search

Issue 25, 2014
Previous Article Next Article

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

Author affiliations

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?

Back to tab navigation

Publication details

The article was received on 20 Feb 2014, accepted on 20 Mar 2014 and first published on 20 May 2014


Article type: Perspective
DOI: 10.1039/C4DT00539B
Citation: Dalton Trans., 2014,43, 9392-9405
  • Open access: Creative Commons BY license
  •   Request permissions

    [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

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements