Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Gudrun C. Hartmann"'
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
https://doi.org/10.1007/s002030050716
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
https://doi.org/10.1002/(sici)1521-3773(19981217)37:23<3300::aid-anie3300>3.0.co
Autor:
Gudrun C. Hartmann, Rolf K. Thauer, Thomas Prasch, Christian Griesinger, Gerrit Buurman, Bernhard H. Geierstanger
Publikováno v:
Angewandte Chemie. 110:3491-3494
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57d32dee0ab5bb2cbde04ae69692d2d4
https://doi.org/10.1002/(sici)1521-3757(19981204)110:23<3491::aid-ange3491>3.0.co
https://doi.org/10.1002/(sici)1521-3757(19981204)110:23<3491::aid-ange3491>3.0.co
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
https://doi.org/10.1007/s007750050077
Publikováno v:
Archives of Microbiology. 165:187-193
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb0c8289fbecd1c2475a0b3aede645bd
https://doi.org/10.1007/s002030050314
https://doi.org/10.1007/s002030050314
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
https://doi.org/10.1111/j.1432-1033.1995.372_1.x
Publikováno v:
ChemInform. 28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1045f86d670fd92c10d529b659716340
https://doi.org/10.1002/chin.199710281
https://doi.org/10.1002/chin.199710281
Publikováno v:
Chemical reviews. 96(7)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0584345669e3d85e1eae2275d8c862a2
https://pubmed.ncbi.nlm.nih.gov/11848851
https://pubmed.ncbi.nlm.nih.gov/11848851