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Cover Picture: Reversible Dimerization of Mononuclear Models of [Fe]‐Hydrogenase (Chem. Eur. J. 20/2013)
Author(s) -
Hu Bowen,
Chen Dafa,
Hu Xile
Publication year - 2013
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201390069
Subject(s) - hydrogenase , ligand (biochemistry) , denticity , chemistry , alkyl , supramolecular chemistry , stereochemistry , combinatorial chemistry , catalysis , molecule , crystallography , receptor , biochemistry , organic chemistry , crystal structure
A unique bidentate pyridinol cofactor is to be found in [Fe]‐hydrogenase. In their Communication on page 6221 ff. , D. Chen, X. Hu, and B. Hu demonstrate the synthesis and reactivities of a series of mononuclear models, including the first five‐coordinate complex with an alkyl thiolate ligand, that mimic the main structure of the [Fe]‐hydrogenase active site. The equilibrium between these models and their dimeric components is also described.