The crystal structure of C176A mutated [Fe]‐hydrogenase suggests an acyl‐iron ligation in the active site iron complex-Reference-Cited by-同舟云学术

The crystal structure of C176A mutated [Fe]‐hydrogenase suggests an acyl‐iron ligation in the active site iron complex

Published:2009-01-20 Issue:3 Volume:583 Page:585-590
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Letters

Author:

Hiromoto Takeshi¹,Ataka Kenichi²,Pilak Oliver¹,Vogt Sonja¹,Stagni Marco Salomone³,Meyer-Klaucke Wolfram³,Warkentin Eberhard⁴,Thauer Rudolf K.¹,Shima Seigo¹,Ermler Ulrich⁴

Affiliation:

1. Max-Planck-Institut für Terrestrische Mikrobiologie, Karl-von-Frisch-Straße, D-35043 Marburg, Germany

2. Bielefeld University, Department of Chemistry, Universitätsstraße 25, D-33615 Bielefeld, Germany

3. EMBL Hamburg, Notkestraße. 85, D-22603 Hamburg, Germany

4. Max-Planck-Institut für Biophysik, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2009.01.017

Reference27 articles.

1. The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

2. Structure/Function Relationships of [NiFe]- and [FeFe]-Hydrogenases

3. A third type of hydrogenase catalyzing H2 activation

4. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas

5. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution

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