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

FEBS Letters

Volumn 583, Issue 3, 2009, Pages 585-590

  Hiromoto, Takeshi ^a   Ataka, Kenichi ^b   Pilak, Oliver ^a   Vogt, Sonja ^a   Stagni, Marco Salomone ^c   Meyer Klaucke, Wolfram ^c   Warkentin, Eberhard ^d   Thauer, Rudolf K ^a   Shima, Seigo ^a   Ermler, Ulrich ^d  

^a MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

^b BIELEFELD UNIVERSITY   (Germany)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^d MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

Hydrogenase; Iron complex; Iron guanylylpyridinol cofactor; Methanogenic archaea; X ray absorption spectroscopy; X ray crystal structure

Indexed keywords

DITHIOTHREITOL; IRON COMPLEX; IRON HYDROGENASE; OXYGEN; PYRIDINOL; SULFUR;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; STRUCTURE ANALYSIS;

ADENINE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYTOSINE; HOLOENZYMES; HYDROGENASE; IRON; IRON-SULFUR PROTEINS; METHANOCOCCALES; MUTATION; PROTEIN STRUCTURE, QUATERNARY;

EID: 58949101261     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.01.017     Document Type: Article

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