English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Thesis

Kristallstruktur von [Fe]-Hydrogenase Hmd.

MPS-Authors
/persons/resource/persons254607

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;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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).