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000087264 1001_ $$0P:(DE-HGF)0$$aHiromoto, Takashi$$b0
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000087264 245__ $$aThe Crystal Structure of C176A Mutated [Fe]-Hydrogenase Suggests an Acyl-Iron Ligation in the Active Site Iron Complex
000087264 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2009
000087264 300__ $$a585-590
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000087264 440_0 $$0PERI:(DE-600)1460391-3$$aFEBS Letters$$v583$$x0014-5793$$y3
000087264 500__ $$3Converted on 2013-05-30 12:56$$a(c) Federation of European Biochemical Societies. Post referee full text in progress (embargo 1 year from 20 JAN 2009).
000087264 500__ $$3Converted on 2013-06-21 19:20
000087264 520__ $$a[Fe]-hydrogenase is one of three types of enzymes known to activate H(2). Crystal structure analysis recently revealed that its active site iron is ligated square-pyramidally by Cys176-sulfur, two CO, an "unknown" ligand and the sp(2)-hybridized nitrogen of a unique iron-guanylylpyridinol-cofactor. We report here on the structure of the C176A mutated enzyme crystallized in the presence of dithiothreitol (DTT). It suggests an iron center octahedrally coordinated by one DTT-sulfur and one DTT-oxygen, two CO, the 2-pyridinol's nitrogen and the 2-pyridinol's 6-formylmethyl group in an acyl-iron ligation. This result led to a re-interpretation of the iron ligation in the wild-type.
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000087264 650_7 $$00$$2NLM Chemicals$$aHoloenzymes
000087264 650_7 $$00$$2NLM Chemicals$$aIron-Sulfur Proteins
000087264 650_7 $$071-30-7$$2NLM Chemicals$$aCytosine
000087264 650_7 $$073-24-5$$2NLM Chemicals$$aAdenine
000087264 650_7 $$07439-89-6$$2NLM Chemicals$$aIron
000087264 650_7 $$0EC 1.12.-$$2NLM Chemicals$$airon hydrogenase
000087264 650_7 $$0EC 1.12.7.2$$2NLM Chemicals$$aHydrogenase
000087264 650_2 $$2MeSH$$aAdenine: metabolism
000087264 650_2 $$2MeSH$$aCatalytic Domain
000087264 650_2 $$2MeSH$$aCrystallography, X-Ray
000087264 650_2 $$2MeSH$$aCytosine: metabolism
000087264 650_2 $$2MeSH$$aHoloenzymes: chemistry
000087264 650_2 $$2MeSH$$aHoloenzymes: genetics
000087264 650_2 $$2MeSH$$aHoloenzymes: metabolism
000087264 650_2 $$2MeSH$$aHydrogenase: chemistry
000087264 650_2 $$2MeSH$$aHydrogenase: genetics
000087264 650_2 $$2MeSH$$aHydrogenase: metabolism
000087264 650_2 $$2MeSH$$aIron: chemistry
000087264 650_2 $$2MeSH$$aIron: metabolism
000087264 650_2 $$2MeSH$$aIron-Sulfur Proteins: chemistry
000087264 650_2 $$2MeSH$$aIron-Sulfur Proteins: genetics
000087264 650_2 $$2MeSH$$aIron-Sulfur Proteins: metabolism
000087264 650_2 $$2MeSH$$aMethanococcales: enzymology
000087264 650_2 $$2MeSH$$aMethanococcales: genetics
000087264 650_2 $$2MeSH$$aMutation: genetics
000087264 650_2 $$2MeSH$$aProtein Structure, Quaternary
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000087264 7001_ $$0P:(DE-HGF)0$$aAtaka, Kenichi$$b1
000087264 7001_ $$0P:(DE-HGF)0$$aPilak, Oliver$$b2
000087264 7001_ $$aVogt, S.$$b3
000087264 7001_ $$0P:(DE-HGF)0$$aSalamone Stagni, Marco$$b4
000087264 7001_ $$0P:(DE-H253)PIP1001970$$aMeyer-Klaucke, W.$$b5
000087264 7001_ $$0P:(DE-HGF)0$$aWarkentin, Eberhard$$b6
000087264 7001_ $$0P:(DE-HGF)0$$aThauer, Rudolf K.$$b7
000087264 7001_ $$0P:(DE-HGF)0$$aShima, Seigo$$b8$$eCorresponding author
000087264 7001_ $$0P:(DE-H253)PIP1018667$$aErmler, U.$$b9$$eCorresponding author
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000087264 9141_ $$a(c) Elsevier. No copyright permission for full text.$$y2009
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