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Journal Article

The Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H2 Activation

MPS-Authors
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Hiromoto,  Takeshi
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons137939

Warkentin,  Eberhard
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons254548

Moll,  Johanna
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons137648

Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137895

Shima,  Seigo
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Hiromoto, T., Warkentin, E., Moll, J., Ermler, U., & Shima, S. (2009). The Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H2 Activation. Angewandte Chemie, International Edition in English, 48(35), 6457-6460. doi:10.1002/anie.200902695.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D7C6-9
Abstract
The structure of a binary complex of C176A [Fe]-hydrogenase with methylenetetrahydromethanopterin was solved at 2.15 Å resolution in an open conformation. A closed form of the complex was modeled on the basis of the experimentally determined structure. In this model, the iron-site trans to the acyl carbon is located next to the C14a and therefore considered as H2 binding site.