English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

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

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. doi:10.1016/j.febslet.2009.01.017.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Hiromoto, Takeshi1, Author
Ataka, Kenichi2, Author
Pilak, Oliver1, Author
Vogt, Sonja1, Author
Stagni, Marco Salomone3, Author
Meyer-Klaucke, Wolfram3, Author
Warkentin, Eberhard4, Author           
Thauer, Rudolf K.1, Author
Shima, Seigo1, Author
Ermler, Ulrich4, Author           
Affiliations:
1Max-Planck-Institut für Terrestrische Mikrobiologie, 35043 Marburg, Germany, ou_persistent22              
2Bielefeld University, Department of Chemistry, 33615 Bielefeld, Germany, ou_persistent22              
3EMBL Hamburg, 22603 Hamburg, Germany, ou_persistent22              
4Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

Content

show
hide
Free keywords: Hydrogenase; Iron–guanylylpyridinol-cofactor; Methanogenic archaea; Iron complex; X-ray crystal structure; X-ray absorption spectroscopy
 Abstract: [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

Details

show
hide
Language(s): eng - English
 Dates: 2008-12-302008-11-202009-01-052009-01-202009-02-04
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.febslet.2009.01.017
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 583 (3) Sequence Number: - Start / End Page: 585 - 590 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501