Premium
Iron‐Chromophore Circular Dichroism of [Fe]‐Hydrogenase: The Conformational Change Required for H 2 Activation
Author(s) -
Shima Seigo,
Vogt Sonja,
Göbels Andreas,
Bill Eckhard
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201006255
Subject(s) - hydrogenase , chromophore , cofactor , circular dichroism , conformational change , chemistry , active site , methylene , crystallography , methylene blue , stereochemistry , catalysis , photochemistry , enzyme , organic chemistry , photocatalysis
CD can see it : [Fe]‐hydrogenase, which contains a unique iron cofactor (FeGP cofactor), catalyzes the reversible hydrogenation of methenyltetrahydrometanopterin (methenyl‐H 4 MPT + ) with H 2 to methylene‐H 4 MPT (see picture). Iron‐chromophore CD data support the hypothesis that the binding of methenyl/methylene‐H 4 MPT induces a conformational change that closes the active‐site cleft of [Fe]‐hydrogenase to form the intact active site.