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Synthesis and Structure of a Biomimetic Model of the Iron Hydrogenase Active Site Covalently Linked to a Ruthenium Photosensitizer

✍ Scribed by Sascha Ott; Mikael Kritikos; Björn Åkermark; Licheng Sun

Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
134 KB
Volume
42
Category
Article
ISSN
0044-8249

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✦ Synopsis

Although known for more than 75 years, [1] sulfur-containing binuclear complexes of iron have recently experienced a renaissance as interesting synthetic targets as they closely resemble the active site of iron hydrogenases (FeH), a naturally occurring class of enzymes which regulate the production and consumption of hydrogen in microorganisms. [2][3][4][5] Crystallographic studies revealed the active site of the natural system to consist of two iron(i) cations which are linked by an unusual bridging dithiolate ligand. [6,7] It has been [*] Prof.

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