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Kristallstruktur von [Fe]-Hydrogenase Hmd.

MPS-Authors
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Pilak,  Oliver
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Pilak, O. (2007). Kristallstruktur von [Fe]-Hydrogenase Hmd. PhD Thesis, Philipps-Universität Marburg, Marburg.


Cite as: https://hdl.handle.net/21.11116/0000-0007-C703-5
Abstract
Hydrogenases, hydrogen-splitting enzymes, are of common interest, because they may substitute platinum as a catalyst for the splitting of hydrogen. [Fe]-hydrogenase is a new type of hydrogenase without a crystal structure available as yet. In this work the crystal structures of [Fe]-hydrogenase apoenzyme, holoenzyme and cyanide-inhibited holoenzyme are presented. [Fe]-hydrogenase is a mononuclear iron enzyme containing a new biological cofactor (FeGP cofactor). The iron in [Fe]-hydrogenase is pentacoordinated (one sulfur, one nitrogen, two CO and one unknown ligand, that can be substituted by cyanide).