| Home > Publications database > The Crystal Structure of C176A Mutated [Fe]-Hydrogenase Suggests an Acyl-Iron Ligation in the Active Site Iron Complex > print |
| 001 | 87264 | ||
| 005 | 20250731122201.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:19162018 |
| 024 | 7 | _ | |2 ISSN |a 1873-3468 |
| 024 | 7 | _ | |2 ISSN |a 0014-5793 |
| 024 | 7 | _ | |2 WOS |a WOS:000263603600014 |
| 024 | 7 | _ | |2 doi |a 10.1016/j.febslet.2009.01.017 |
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| 037 | _ | _ | |a PHPPUBDB-8575 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Hiromoto, Takashi |b 0 |
| 110 | 1 | _ | |a DESY |b Experiments with synchrotron radiation |
| 245 | _ | _ | |a The Crystal Structure of C176A Mutated [Fe]-Hydrogenase Suggests an Acyl-Iron Ligation in the Active Site Iron Complex |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2009 |
| 300 | _ | _ | |a 585-590 |
| 336 | 7 | _ | |2 DRIVER |a article |
| 336 | 7 | _ | |2 DataCite |a Output Types/Journal article |
| 336 | 7 | _ | |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |a Journal Article |b journal |m journal |s 1481730256_13084 |
| 336 | 7 | _ | |2 BibTeX |a ARTICLE |
| 336 | 7 | _ | |2 ORCID |a JOURNAL_ARTICLE |
| 336 | 7 | _ | |0 0 |2 EndNote |a Journal Article |
| 440 | _ | 0 | |0 PERI:(DE-600)1460391-3 |a FEBS Letters |v 583 |x 0014-5793 |y 3 |
| 500 | _ | _ | |3 Converted 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). |
| 500 | _ | _ | |3 Converted on 2013-06-21 19:20 |
| 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. |
| 536 | _ | _ | |0 G:(DE-H253)POF1-No-Ref-20130405 |f POF I |x 0 |c POF1-550 |a FS Beamline without reference (POF1-550) |
| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Holoenzymes |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Iron-Sulfur Proteins |
| 650 | _ | 7 | |0 71-30-7 |2 NLM Chemicals |a Cytosine |
| 650 | _ | 7 | |0 73-24-5 |2 NLM Chemicals |a Adenine |
| 650 | _ | 7 | |0 7439-89-6 |2 NLM Chemicals |a Iron |
| 650 | _ | 7 | |0 EC 1.12.- |2 NLM Chemicals |a iron hydrogenase |
| 650 | _ | 7 | |0 EC 1.12.7.2 |2 NLM Chemicals |a Hydrogenase |
| 650 | _ | 2 | |2 MeSH |a Adenine: metabolism |
| 650 | _ | 2 | |2 MeSH |a Catalytic Domain |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Cytosine: metabolism |
| 650 | _ | 2 | |2 MeSH |a Holoenzymes: chemistry |
| 650 | _ | 2 | |2 MeSH |a Holoenzymes: genetics |
| 650 | _ | 2 | |2 MeSH |a Holoenzymes: metabolism |
| 650 | _ | 2 | |2 MeSH |a Hydrogenase: chemistry |
| 650 | _ | 2 | |2 MeSH |a Hydrogenase: genetics |
| 650 | _ | 2 | |2 MeSH |a Hydrogenase: metabolism |
| 650 | _ | 2 | |2 MeSH |a Iron: chemistry |
| 650 | _ | 2 | |2 MeSH |a Iron: metabolism |
| 650 | _ | 2 | |2 MeSH |a Iron-Sulfur Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Iron-Sulfur Proteins: genetics |
| 650 | _ | 2 | |2 MeSH |a Iron-Sulfur Proteins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Methanococcales: enzymology |
| 650 | _ | 2 | |2 MeSH |a Methanococcales: genetics |
| 650 | _ | 2 | |2 MeSH |a Mutation: genetics |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Quaternary |
| 693 | _ | _ | |0 EXP:(DE-H253)Unknown-BL-20150101 |6 EXP:(DE-H253)Unknown-BL-20150101 |f Unknown DESY Beamline |x 0 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Ataka, Kenichi |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Pilak, Oliver |b 2 |
| 700 | 1 | _ | |a Vogt, S. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Salamone Stagni, Marco |b 4 |
| 700 | 1 | _ | |0 P:(DE-H253)PIP1001970 |a Meyer-Klaucke, W. |b 5 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Warkentin, Eberhard |b 6 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Thauer, Rudolf K. |b 7 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Shima, Seigo |b 8 |e Corresponding author |
| 700 | 1 | _ | |0 P:(DE-H253)PIP1018667 |a Ermler, U. |b 9 |e Corresponding author |
| 773 | _ | _ | |0 PERI:(DE-600)1460391-3 |a 10.1016/j.febslet.2009.01.017 |g Vol. 583, p. 585-590 |p 585-590 |q 583<585-590 |t FEBS letters |v 583 |x 0014-5793 |y 2009 |
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| 913 | 1 | _ | |0 G:(DE-HGF)POF1-550 |9 G:(DE-H253)POF1-No-Ref-20130405 |v Großgeräte für die Forschung mit Photonen, Neutronen, Ionen |x 0 |a DE-H253 |4 G:(DE-HGF)POF |1 G:(DE-HGF)POF1-550 |3 G:(DE-HGF)POF1 |2 G:(DE-HGF)POF1-500 |b Struktur der Materie |l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen |
| 914 | 1 | _ | |a (c) Elsevier. No copyright permission for full text. |y 2009 |
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