Works by Thauer, Rudolf K.

Results: 54
    1
    2
    3
    4

    A Nickel–Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane FormationWe thank the Swiss National Science Foundation (SNF) and the Fonds der Chemischen Industrie for financial support. D.H. gratefully acknowledges a research scholarship (HI 1094/1-1) from the Deutsche Forschungsgemeinschaft (DFG). We are grateful to Brian M. Hoffman (Northwestern Univ.) for helpful discussions.

    Published in:
    Angewandte Chemie, 2006, v. 118, n. 22, p. 3684, doi. 10.1002/ange.200600366
    By:
    • Dariush Hinderberger;
    • Rafal P. Piskorski;
    • Meike Goenrich;
    • Rudolf K. Thauer;
    • Arthur Schweiger;
    • Jeffrey Harmer;
    • Bernhard Jaun
    Publication type:
    Article
    5

    The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light-Inactivation Product ( The authors thank Prof. Dr. Stefan Berger (Universität Leipzig) for the determination of the high-resolution mass data, Dr. Stefan Bartoschek and Dr. Peter Grice (University of Cambridge, UK) for recording the broadband <sup>13</sup>C NMR spectrum on a <sup>13</sup>C detection cryoprobe, Prof. Dr. Thomas Carell (Universität Marburg) for helpful discussions, and Dr. Antonio Pierik for assistance with the fluorescence measurements. L.V. was funded by the European research network HPRN CT 2000 00092. )

    Published in:
    Angewandte Chemie, 2004, v. 116, n. 19, p. 2601, doi. 10.1002/ange.200353763
    By:
    • Seigo Shima;
    • Erica J. Lyon;
    • Melanie Sordel-Klippert;
    • Manuela Kauß;
    • Jörg Kahnt;
    • Rudolf K. Thauer;
    • Klaus Steinbach;
    • Xiulan Xie;
    • Laurent Verdier;
    • Christian Griesinger
    Publication type:
    Article
    6
    7
    8
    9
    10
    11
    12
    13
    14
    15
    16
    17
    18
    19
    20
    21

    Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F<sub>420</sub>: Architecture of the F<sub>420</sub>/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family.

    Published in:
    Protein Science: A Publication of the Protein Society, 2005, v. 14, n. 7, p. 1840, doi. 10.1110/ps.041289805
    By:
    • Aufhammer, Stephan W.;
    • Warkentin, Eberhard;
    • Ermler, Ulrich;
    • Hagemeier, Christoph H.;
    • Thauer, Rudolf K.;
    • Shima, Seigo
    Publication type:
    Article
    22
    23
    24
    25
    26
    27

    Cover Picture.

    Published in:
    ChemBioChem, 2001, v. 2, n. 7/8, p. 473, doi. 10.1002/1439-7633(20010803)2:7/8&lt;473::AID-CBIC473&gt;3.0.CO;2-D
    By:
    • Bartoschek, Stefan;
    • Buurman, Gerrit;
    • Thauer, Rudolf K.;
    • Geierstanger, Bernhard H.;
    • Weyrauch, Jan P.;
    • Griesinger, Christian;
    • Nilges, Michael;
    • Hutter, Michael C.;
    • Helms, Volkhard
    Publication type:
    Article
    28

    A Nickel–Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane FormationWe thank the Swiss National Science Foundation (SNF) and the Fonds der Chemischen Industrie for financial support. D.H. gratefully acknowledges a research scholarship (HI 1094/1-1) from the Deutsche Forschungsgemeinschaft (DFG). We are grateful to Brian M. Hoffman (Northwestern Univ.) for helpful discussions.

    Published in:
    Angewandte Chemie International Edition, 2006, v. 45, n. 22, p. 3602, doi. 10.1002/anie.200600366
    By:
    • Dariush Hinderberger;
    • Rafal P. Piskorski;
    • Meike Goenrich;
    • Rudolf K. Thauer;
    • Arthur Schweiger;
    • Jeffrey Harmer;
    • Bernhard Jaun
    Publication type:
    Article
    29

    The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light-Inactivation Product ( The authors thank Prof. Dr. Stefan Berger (Universität Leipzig) for the determination of the high-resolution mass data, Dr. Stefan Bartoschek and Dr. Peter Grice (University of Cambridge, UK) for recording the broadband <sup>13</sup>C NMR spectrum on a <sup>13</sup>C detection cryoprobe, Prof. Dr. Thomas Carell (Universität Marburg) for helpful discussions, and Dr. Antonio Pierik for assistance with the fluorescence measurements. L.V. was funded by the European research network HPRN CT 2000 00092. )

    Published in:
    Angewandte Chemie International Edition, 2004, v. 43, n. 19, p. 2547, doi. 10.1002/anie.200353763
    By:
    • Seigo Shima;
    • Erica J. Lyon;
    • Melanie Sordel-Klippert;
    • Manuela Kauß;
    • Jörg Kahnt;
    • Rudolf K. Thauer;
    • Klaus Steinbach;
    • Xiulan Xie;
    • Laurent Verdier;
    • Christian Griesinger
    Publication type:
    Article
    30
    31
    32
    33
    34
    35
    36
    37
    38
    39
    40
    41
    42
    43
    44
    45
    46
    47
    48
    49
    50

    Spectroscopic investigation of the nickel-containing porphinoid cofactor F<sub>430</sub>. Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms.

    Published in:
    Journal of Biological Inorganic Chemistry (JBIC), 2004, v. 9, n. 5, p. 563, doi. 10.1007/s00775-004-0549-9
    By:
    • Duin, Evert C.;
    • Signor, Luca;
    • Piskorski, Rafal;
    • Mahlert, Felix;
    • Clay, Michael D.;
    • Goenrich, Meike;
    • Thauer, Rudolf K.;
    • Jaun, Bernhard;
    • Johnson, Michael K.
    Publication type:
    Article