Journal
COORDINATION CHEMISTRY REVIEWS
Volume 249, Issue 15-16, Pages 1653-1663Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2005.01.013
Keywords
bioinorganic chemistry; electron transfer; enzyme models; iron hydrogenase; ruthenium
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Models of the iron hydrogenase active site [(mu-DT)Fe-2(CO)(6)] (DT: dithiolate) have been synthesized where the dithiolate co-factor bears a functional group to allow for their incorporation into supramolecular systems. Covalently linked to ruthenium(II) polypyridyl photosensitizers, the resulting ruthenium-diiron complexes represent the first members of a new class of dyads designed to promote the light-driven production of hydrogen. The functionalized diiron complexes have been characterized by X-ray crystallography. The redox properties of all complexes were investigated by cyclic voltammetry and the interactions between the photo-excited ruthenium moiety and the diiron unit in these dyads were evaluated by time-resolved spectroscopy. (c) 2005 Elsevier B.V. All rights reserved.
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