Works by Thauer, Rudolf K.
Results: 54
The Physiological Role of the Ribulose Monophosphate Pathway in Bacteria and Archaea.
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- Bioscience, Biotechnology & Biochemistry, 2006, v. 70, n. 1, p. 10, doi. 10.1271/bbb.70.10
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- Article
Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Struktur des porphinoiden Ligandsystems.
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- Helvetica Chimica Acta, 1982, v. 65, n. 3, p. 828, doi. 10.1002/hlca.19820650320
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- Article
Structures of F<sub>420</sub>H<sub>2</sub>:NADP<sup>+</sup> oxidoreductase with and without its substrates bound.
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- EMBO Journal, 2001, v. 20, n. 23, p. 6561, doi. 10.1093/emboj/20.23.6561
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- Article
The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane.
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- Nature, 2010, v. 465, n. 7298, p. 606, doi. 10.1038/nature09015
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- Article
Biogeochemistry: Methane and microbes.
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- Nature, 2006, v. 440, n. 7086, p. 878, doi. 10.1038/440878a
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- Article
Dual Role of S-Adenosylmethionine (SAM<sup>+</sup>) in the Methylation of sp<sup>2</sup>-Hybridized Electrophilic Carbons.
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- Angewandte Chemie International Edition, 2011, v. 50, n. 45, p. 10492, doi. 10.1002/anie.201105076
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- Article
Intermediates in the Catalytic Cycle of Methyl Coenzyme M Reductase: Isotope Exchange is Consistent with Formation of a σ-Alkane-Nickel Complex.
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- Angewandte Chemie International Edition, 2010, v. 49, n. 44, p. 8112, doi. 10.1002/anie.201003214
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- Article
Functionalization of Methane in Anaerobic Microorganisms.
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- Angewandte Chemie International Edition, 2010, v. 49, n. 38, p. 6712, doi. 10.1002/anie.201002967
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- Article
Methanogenic archaea: ecologically relevant differences in energy conservation.
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- Nature Reviews Microbiology, 2008, v. 6, n. 8, p. 579, doi. 10.1038/nrmicro1931
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- Article
Re-Face Stereospecificity of Methylenetetrahydromethanopterin and Methylenetetrahydrofolate Dehydrogenases is Predetermined by Intrinsic Properties of the Substrate.
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- ChemBioChem, 2001, v. 2, n. 7/8, p. 530, doi. 10.1002/1439-7633(20010803)2:7/8<530::AID-CBIC530>3.0.CO;2-0
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Cover Picture.
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- ChemBioChem, 2001, v. 2, n. 7/8, p. 473, doi. 10.1002/1439-7633(20010803)2:7/8<473::AID-CBIC473>3.0.CO;2-D
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- Article
Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase.
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- Journal of Biological Inorganic Chemistry (JBIC), 2008, v. 13, n. 8, p. 1275, doi. 10.1007/s00775-008-0417-0
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- Article
The exchange activities of [Fe] hydrogenase (iron–sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases.
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- Journal of Biological Inorganic Chemistry (JBIC), 2008, v. 13, n. 1, p. 97, doi. 10.1007/s00775-007-0302-2
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Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy.
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- Journal of Biological Inorganic Chemistry (JBIC), 2007, v. 12, n. 8, p. 1097, doi. 10.1007/s00775-007-0281-3
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Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues.
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- Journal of Biological Inorganic Chemistry (JBIC), 2004, v. 9, n. 6, p. 691, doi. 10.1007/s00775-004-0552-1
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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.
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- Journal of Biological Inorganic Chemistry (JBIC), 2004, v. 9, n. 5, p. 563, doi. 10.1007/s00775-004-0549-9
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Characterization of the MCR<sub>red2</sub> form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study.
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- Journal of Biological Inorganic Chemistry (JBIC), 2003, v. 8, n. 5, p. 586, doi. 10.1007/s00775-003-0450-y
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Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy.
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- Journal of Biological Inorganic Chemistry (JBIC), 2003, v. 8, n. 1/2, p. 141, doi. 10.1007/s00775-002-0399-2
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Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically.
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- Nature, 2012, v. 481, n. 7379, p. 98, doi. 10.1038/nature10663
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More Than 200 Genes Required for Methane Formation from H<sub>2</sub> and CO<sub>2</sub> and Energy Conservation Are Present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus.
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- Archaea, 2011, p. 1, doi. 10.1155/2011/973848
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- Article
Lothar Jaenicke and C<sub>1</sub>-metabolism: his first 25 years of research.
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- Zeitschrift für Naturforschung. Section C: A Journal of Biosciences, 2017, v. 72, n. 7/8, p. 237, doi. 10.1515/znc-2017-0108
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The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex
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- FEBS Letters, 2009, v. 583, n. 3, p. 585, doi. 10.1016/j.febslet.2009.01.017
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The CO and CN<sup>−</sup> ligands to the active site Fe in [NiFe]-hydrogenase of Escherichia coli have different metabolic origins
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- FEBS Letters, 2007, v. 581, n. 17, p. 3317, doi. 10.1016/j.febslet.2007.06.028
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F<sub>420</sub>H<sub>2</sub> oxidase (FprA) fromMethanobrevibacter arboriphilus, a coenzyme F<sub>420</sub>-dependent enzyme involved in O<sub>2</sub> detoxification.
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- Archives of Microbiology, 2004, v. 182, n. 2/3, p. 126, doi. 10.1007/s00203-004-0675-3
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Regulation of the synthesis of H<sub>2</sub>-forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of HmdII and HmdIII in Methanothermobacter marburgensis.
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- 2000
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- Erratum
Regulation of the synthesis of H<sub>2</sub>-forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of HmdII and HmdIII in Methanothermobacter marburgensis.
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- Archives of Microbiology, 2000, v. 174, n. 4, p. 225, doi. 10.1007/s002030000197
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Protection of Methanosarcina barkeri against oxidative stress: identification and characterization of an iron superoxide dismutase.
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- Archives of Microbiology, 2000, v. 174, n. 3, p. 213, doi. 10.1007/s002030000180
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Flavin-Based Electron Bifurcation, Ferredoxin, Flavodoxin, and Anaerobic Respiration With Protons (Ech) or NAD<sup>+</sup> (Rnf) as Electron Acceptors: A Historical Review.
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- Frontiers in Microbiology, 2018, p. 1, doi. 10.3389/fmicb.2018.00401
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On the Mechanism of Catalysis by a Metal-Free Hydrogenase from Methanogenic Archaea: Enzymatic Transformation of H<sub>2</sub> without a Metal and Its Analogy to the Chemistry of Alkanes in Superacidic Solution.
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- Angewandte Chemie International Edition, 1995, v. 34, n. 20, p. 2247, doi. 10.1002/anie.199522471
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Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri.
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- Proteins, 1996, v. 26, n. 1, p. 118, doi. 10.1002/(SICI)1097-0134(199609)26:1<118::AID-PROT12>3.0.CO;2-J
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Nickelenzyme im Stoffwechsel von methanogenen Bakterien.
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- Biological Chemistry, 1985, v. 366, n. 1, p. 103
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Methane as Fuel for Anaerobic Microorganisms.
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- Annals of the New York Academy of Sciences, 2008, v. 1125, p. 158, doi. 10.1196/annals.1419.000
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- Article
Doppelte Rolle von S-Adenosylmethionin (SAM<sup>+</sup>) bei der Methylierung von sp<sup>2</sup>-hybridisierten elektrophilen Kohlenstoffatomen.
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- Angewandte Chemie, 2011, v. 123, n. 45, p. 10676, doi. 10.1002/ange.201105076
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- Article
Zwischenprodukte im Katalysezyklus von Methyl-Coenzym-M- Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines σ-Alkan-Nickel-Komplexes.
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- Angewandte Chemie, 2010, v. 122, n. 44, p. 8289, doi. 10.1002/ange.201003214
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Funktionalisierung von Methan in anaeroben Mikroorganismen.
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- Angewandte Chemie, 2010, v. 122, n. 38, p. 6862, doi. 10.1002/ange.201002967
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- Article
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.
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- Angewandte Chemie, 2006, v. 118, n. 22, p. 3684, doi. 10.1002/ange.200600366
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- Article
The Cofactor of the IronSulfur 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. )
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- Angewandte Chemie, 2004, v. 116, n. 19, p. 2601, doi. 10.1002/ange.200353763
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A third type of hydrogenase catalyzing H<sub>2</sub> activation.
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- Chemical Record, 2007, v. 7, n. 1, p. 37, doi. 10.1002/tcr.20111
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Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea.
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- FEBS Journal, 2007, v. 274, n. 18, p. 4913, doi. 10.1111/j.1742-4658.2007.06016.x
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Structure of coenzyme F<sub>420</sub>H<sub>2</sub> oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O<sub>2</sub> to H<sub>2</sub>O.
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- FEBS Journal, 2007, v. 274, n. 6, p. 1588, doi. 10.1111/j.1742-4658.2007.05706.x
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Si-face stereospecificity at C5 of coenzyme F<sub>420</sub> for F<sub>420</sub>H<sub>2</sub> oxidase from methanogenic Archaea as determined by mass spectrometry.
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- FEBS Journal, 2005, v. 272, n. 20, p. 5337, doi. 10.1111/j.1742-4658.2005.04931.x
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- Article
Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Über die Natur der Isolierungsartefakte von F430, ein Beitrag zur Chemie von F430 und zur konformationellen Stereochemie der Ligandperipherie von hydroporphinoiden Nickel(II)-Komplexen.
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- Helvetica Chimica Acta, 1985, v. 68, n. 5, p. 1338, doi. 10.1002/hlca.19850680527
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Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Struktur des proteinfreien Faktors.
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- Helvetica Chimica Acta, 1984, v. 67, n. 1, p. 334, doi. 10.1002/hlca.19840670141
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A conspicuous nickel protein in microbial mats that oxidize methane anaerobically.
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- Nature, 2003, v. 426, n. 6968, p. 878, doi. 10.1038/nature02207
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- Article
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.
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- Angewandte Chemie International Edition, 2006, v. 45, n. 22, p. 3602, doi. 10.1002/anie.200600366
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- Article
The Cofactor of the IronSulfur 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. )
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- Angewandte Chemie International Edition, 2004, v. 43, n. 19, p. 2547, doi. 10.1002/anie.200353763
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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.
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- Protein Science: A Publication of the Protein Society, 2005, v. 14, n. 7, p. 1840, doi. 10.1110/ps.041289805
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Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: A glycerol-3-phosphate dehydrogenase with an unusual NADP<sup>+</sup> preference.
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- Protein Science: A Publication of the Protein Society, 2004, v. 13, n. 12, p. 3161, doi. 10.1110/ps.04980304
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Crystal structures and enzymatic properties of three formyltransferases from archaea: Environmental adaptation and evolutionary relationship.
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- Protein Science: A Publication of the Protein Society, 2002, v. 11, n. 9, p. 2168, doi. 10.1110/ps.0211002
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- Article
Polymer/Bacteria Composite Nanofiber Nonwovens by Electrospinning of Living Bacteria Protected by Hydrogel Microparticles.
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- Macromolecular Bioscience, 2011, v. 11, n. 3, p. 333, doi. 10.1002/mabi.201000310
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- Article