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

被引：175

作者：

Hiromoto, Takeshi ^{[1
]}

Ataka, Kenichi ^{[2
]}

Pilak, Oliver ^{[1
]}

Vogt, Sonja ^{[1
]}

Stagni, Marco Salomone ^{[3
]}

Meyer-Klaucke, Wolfram ^{[3
]}

Warkentin, Eberhard ^{[4
]}

Thauer, Rudolf K. ^{[1
]}

Shima, Seigo ^{[1
]}

Ermler, Ulrich ^{[4
]}

机构：

[1] Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany

[2] Univ Bielefeld, Dept Chem, D-33615 Bielefeld, Germany

[3] EMBL Hamburg, D-22603 Hamburg, Germany

[4] Max Planck Inst Biophys, D-60438 Frankfurt, Germany

来源：

FEBS LETTERS | 2009年 / 583卷 / 03期

关键词：

Hydrogenase; Iron-guanylylpyridinol-cofactor; Methanogenic archaea; Iron complex; X-ray crystal structure; X-ray absorption spectroscopy; CLUSTER-FREE HYDROGENASE; METAL-FREE HYDROGENASE; METHANOGENIC ARCHAEA; LIGHT-INACTIVATION; CO DEHYDROGENASE; DIFFRACTION DATA; HMD; REFINEMENT; NICKEL;

D O I：

10.1016/j.febslet.2009.01.017

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

[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 acyliron ligation. This result led to a re-interpretation of the iron ligation in the wild-type. (c) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：585 / 590

页数：6

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