A Pyridinol Acyl Cofactor in the Active Site of [Fe]‐hydrogenase Evidenced by the Reactivity of Model Complexes | Zendy

Hu Bowen | Zendy; Chen Dafa | Zendy; Hu Xile | Zendy

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A Pyridinol Acyl Cofactor in the Active Site of [Fe]‐hydrogenase Evidenced by the Reactivity of Model Complexes

Author(s) -

Hu Bowen,

Chen Dafa,

Hu Xile

Publication year - 2012

Publication title -

chemistry – a european journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.687

H-Index - 242

eISSN - 1521-3765

pISSN - 0947-6539

DOI - 10.1002/chem.201201954

Subject(s) - hydrogenase , moiety , cofactor , denticity , chemistry , ligand (biochemistry) , reactivity (psychology) , stereochemistry , decomposition , combinatorial chemistry , enzyme , organic chemistry , biochemistry , receptor , medicine , alternative medicine , pathology , crystal structure

Understanding the complex : The decomposition reaction of a water‐soluble complex (see scheme; 1 ) in H 2 O confirms the existence of a unique bidentate pyridinol cofactor in [Fe]‐hydrogenase. This unique moiety is confirmed for the first time by the decomposition of a well‐defined model complex containing a pyridinyl methyl acyl ligand.

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