%0 Journal Article
%A Hiromoto, Takashi
%A Ataka, Kenichi
%A Pilak, Oliver
%A Vogt, S.
%A Salamone Stagni, Marco
%A Meyer-Klaucke, W.
%A Warkentin, Eberhard
%A Thauer, Rudolf K.
%A Shima, Seigo
%A Ermler, U.
%A DESY
%T The Crystal Structure of C176A Mutated [Fe]-Hydrogenase Suggests an Acyl-Iron Ligation in the Active Site Iron Complex
%J FEBS letters
%V 583
%@ 0014-5793
%C Amsterdam [u.a.]
%I Elsevier
%M PHPPUBDB-8575
%P 585-590
%D 2009
%Z (c) Federation of European Biochemical Societies. Post referee full text in progress (embargo 1 year from 20 JAN 2009).
%X [Fe]-hydrogenase is one of three types of enzymes known to activate H(2). Crystal structure analysis recently revealed that its active site iron is ligated square-pyramidally by Cys176-sulfur, two CO, an ünknown" ligand and the sp(2)-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 DTT-oxygen, two CO, the 2-pyridinol's nitrogen and the 2-pyridinol's 6-formylmethyl group in an acyl-iron ligation. This result led to a re-interpretation of the iron ligation in the wild-type.
%K Adenine: metabolism
%K Catalytic Domain
%K Crystallography, X-Ray
%K Cytosine: metabolism
%K Holoenzymes: chemistry
%K Holoenzymes: genetics
%K Holoenzymes: metabolism
%K Hydrogenase: chemistry
%K Hydrogenase: genetics
%K Hydrogenase: metabolism
%K Iron: chemistry
%K Iron: metabolism
%K Iron-Sulfur Proteins: chemistry
%K Iron-Sulfur Proteins: genetics
%K Iron-Sulfur Proteins: metabolism
%K Methanococcales: enzymology
%K Methanococcales: genetics
%K Mutation: genetics
%K Protein Structure, Quaternary
%K Holoenzymes (NLM Chemicals)
%K Iron-Sulfur Proteins (NLM Chemicals)
%K Cytosine (NLM Chemicals)
%K Adenine (NLM Chemicals)
%K Iron (NLM Chemicals)
%K iron hydrogenase (NLM Chemicals)
%K Hydrogenase (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19162018
%U <Go to ISI:>//WOS:000263603600014
%R 10.1016/j.febslet.2009.01.017
%U https://bib-pubdb1.desy.de/record/87264