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

MPG-Autoren
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Hiromoto,  Takeshi
Max Planck Institute of Biophysics, Max Planck Society;

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Pilak,  Oliver
Max Planck Institute of Biophysics, Max Planck Society;

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Vogt,  Sonja
Max Planck Institute of Biophysics, Max Planck Society;

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

Thauer,  Rudolf K.
Max Planck Society;

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Shima,  Seigo
Max Planck Institute of Biophysics, Max Planck Society;

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

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Zitation

Hiromoto, T., Ataka, K., Pilak, O., Vogt, S., Stagni, M. S., Meyer-Klaucke, W., et al. (2009). The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Letters, 583(3), 585-590.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-D7C8-5
Zusammenfassung
[Fe]-hydrogenase is one of three types of enzymes known to activate H2. Crystal structure analysis recently revealed that its active site iron is ligated square-pyramidally by Cys176-sulfur, two CO, an ‘‘unknown” ligand and the sp2-hybridized nitrogen of a unique iron–guanylylpyridinol-cofactor. We report here on the structure of the C176A mutated enzyme crystallized in the presence of dithiothreitol (DTT). It suggests an iron center octahedrally coordinated by one DTT-sulfur and one DTToxygen, two CO, the 2-pyridinol’s nitrogen and the 2-pyridinol’s 6-formylmethyl group in an acyliron ligation. This result led to a re-interpretation of the iron ligation in the wild-type