Iron‐Chromophore Circular Dichroism of [Fe]‐Hydrogenase: The Conformational Change Required for H 2  Activation | Zendy

Shima Seigo | Zendy; Vogt Sonja | Zendy; Göbels Andreas | Zendy; Bill Eckhard | Zendy

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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.

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