Journal Article

PHPPUBDB-8575

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png 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. ; Salamone Stagni, M. ; Meyer-Klaucke, W.Extern* ; Warkentin, E. ; Thauer, R. K. ; Shima, S. (Corresponding author) ; Ermler, U. (Corresponding author)Extern* ; DESY

2009
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.febslet.2009.01.017

Abstract: [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 "unknown" 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.

Keyword(s): Adenine: metabolism (MeSH) ; Catalytic Domain (MeSH) ; Crystallography, X-Ray (MeSH) ; Cytosine: metabolism (MeSH) ; Holoenzymes: chemistry (MeSH) ; Holoenzymes: genetics (MeSH) ; Holoenzymes: metabolism (MeSH) ; Hydrogenase: chemistry (MeSH) ; Hydrogenase: genetics (MeSH) ; Hydrogenase: metabolism (MeSH) ; Iron: chemistry (MeSH) ; Iron: metabolism (MeSH) ; Iron-Sulfur Proteins: chemistry (MeSH) ; Iron-Sulfur Proteins: genetics (MeSH) ; Iron-Sulfur Proteins: metabolism (MeSH) ; Methanococcales: enzymology (MeSH) ; Methanococcales: genetics (MeSH) ; Mutation: genetics (MeSH) ; Protein Structure, Quaternary (MeSH) ; Holoenzymes ; Iron-Sulfur Proteins ; Cytosine ; Adenine ; Iron ; iron hydrogenase ; Hydrogenase

Note: (c) Federation of European Biochemical Societies. Post referee full text in progress (embargo 1 year from 20 JAN 2009).

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Contributing Institute(s):

1. Experiments with synchrotron radiation (HASYLAB(-2012))
2. EMBL (EMBL(-2012))

Research Program(s):

1. FS Beamline without reference (POF1-550) (POF1-550)

Experiment(s):

1. Unknown DESY Beamline

Appears in the scientific report 2009
Notes: (c) Elsevier. No copyright permission for full text.

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Database coverage:
; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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