Introducing a dark reaction to photochemistry: photocatalytic hydrogen from [FeFe] hydrogenase active site model complexes

Dalton Trans. 2009 Dec 7:(45):9952-9. doi: 10.1039/b911129h. Epub 2009 Sep 8.

Abstract

The light-driven splitting of water into its constituting elements gives access to a valuable fuel from an abundant substrate, using sunlight as the only energy source. Synthetic diiron complexes as functional models of the [FeFe] hydrogenase H2ase enzyme active site have moved into the centre of focus as potentially viable catalysts for the reductive side of this process, i.e. the reduction of protons to molecular hydrogen. The active site of the enzyme, as well as its mimics in an artificial system, are required to accumulate two electrons from single electron transfer events and to combine them with two protons to form hydrogen. Whereas in biology this reaction is not coupled to photosynthesis and thus proceeds in the dark, additional aspects need to be considered when designing a functional artificial system for the light-driven reduction of protons. Suitable photosensitizers have to be chosen that not only provide sufficient driving force for the reduction of the synthetic diiron catalyst, but also allow for selective excitation to minimize photodegradation. Electron transfer efficiencies have to be optimized for all steps and the sequential nature of the catalyst reduction requires a sufficient stability of potentially labile intermediates of the catalytic cycle. In this perspective, systems for the light-driven conversion of protons to molecular hydrogen are discussed where the catalyst is based on model complexes of the [FeFe] H2ase active site. Covalently linked dyads, supramolecular assemblies and multi-component systems will be examined with an emphasis on mechanistic electron transfer schemes, the properties of the individual components, their scope and their potential limitations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Catalytic Domain
  • Hydrogenase / chemistry*
  • Iron-Sulfur Proteins / chemistry*
  • Models, Biological*
  • Photochemistry*

Substances

  • Iron-Sulfur Proteins
  • Hydrogenase