Zobrazeno 1 - 10 of 13 pro vyhledávání: '"Gudrun C. Hartmann"'
1
Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri
Autor: Alexander I. Netrusov, Seigo Shima, Rudolf K. Thauer, Michaela Wicke, Melanie Sordel, Gudrun C. Hartmann
Publikováno v: Archives of Microbiology. 171:317-323
Methanosarcina barkeri is a strictly anaerobic, cytochrome-containing, methane-forming archaeon. We report here that the microorganism contains a catalase, which was purified and characterized. The enzyme with an apparent molecular mass of 190 kDa wa
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c96158e5dbacc8e46e37edea43ee48f
https://doi.org/10.1007/s002030050716
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2
Catalytic Mechanism of the Metal-Free Hydrogenase from Methanogenic Archaea: Reversed Stereospecificity of the Catalytic and Noncatalytic Reaction
Autor: Gudrun C. Hartmann, Gerrit Buurman, Thomas Prasch, Rolf K. Thauer, Christian Griesinger, Bernhard H. Geierstanger
Publikováno v: Angewandte Chemie International Edition. 37:3300-3303
By activation of the hydrogen acceptor, the metal-free hydrogenase from methanogenic archaea catalyzes the reduction of methenyl tetrahydromethanopterin with H2 . According to NMR spectroscopic analysis of the conformation of the hydrogen acceptor in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::10f35c3a95615561681e80c85a7a2067
https://doi.org/10.1002/(sici)1521-3773(19981217)37:23<3300::aid-anie3300>3.0.co
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4
Studies on the catalytic mechanism of H2-forming methylenetetrahydromethanopterin dehydrogenase: para-ortho H2 conversion rates in H2O and D2O
Autor: Rudolf K. Thauer, Elena Santamaria, Victor M. Fernandez, Gudrun C. Hartmann
Publikováno v: JBIC Journal of Biological Inorganic Chemistry. 1:446-450
H2–forming N5,N10–methylenetetrahydromethanopterin dehydrogenase is a novel type of hydrogenase that contains neither nickel nor iron-sulfur clusters. Evidence has been presented that the reaction mechanism catalyzed by the enzyme is very similar
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0b0d24bec796fb3c65e6658b5ceadc69
https://doi.org/10.1007/s007750050077
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6
Hydrogen Isotope Effects in the Reactions Catalyzed by H2-forming N5,N10-Methylenetetrahydromethanopterin Dehydrogenase from Methanogenic Archaea
Autor: Rudolf K. Thauer, Gudrun C. Hartmann, Andreas R. Klein
Publikováno v: European Journal of Biochemistry. 233:372-376
H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea, which is a novel hydrogenase containing neither nickel nor iron-sulfur clusters, catalyzes the reversible reduction of N5,N10-methenyltetrahydomethanopterin (
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d587dce97c0a0e8fbfe1dc128314638
https://doi.org/10.1111/j.1432-1033.1995.372_1.x
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9
Akademický článek
Hydrogen isotope effects in the reactions catalyzed by H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea.
Autor: Klein, Andreas R.1, Hartmann, Gudrun C.1, Thauer, Rudolf K.1
Publikováno v: European Journal of Biochemistry. 10/1/95, Vol. 233 Issue 1, p372-376. 5p.
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