Publikationen von Meike Goenrich
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Zeitschriftenartikel (22)
Zeitschriftenartikel
135 (40), S. 14985 - 14995 (2013)
Methyl-coenzyme M reductase from Methanogenic archaea: Isotope effects on label exchange and ethane formation with the homologous substrate ethyl-coenzyme M. Journal of the American Chemical Society
Zeitschriftenartikel
135 (40), S. 14975 - 14984 (2013)
Methyl-coenzyme M reductase from Methanogenic archaea: Isotope effects on the formation and anaerobic oxidation of methane. Journal of the American Chemical Society
Zeitschriftenartikel
7 (3), e33439 (2012)
An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis. PLOS ONE
Zeitschriftenartikel
More than 200 genes required for methane formation from H2 and CO2 and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus. Archaea, 973848 (2011)
Zeitschriftenartikel
192 (21), S. 5850 - 5851 (2010)
Complete genome sequence of Methanothermobacter marburgensis, a Methanoarchaeon model organism. Journal of Bacteriology
Zeitschriftenartikel
465 (7298), S. 606 - U97 (2010)
The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane. Nature
Zeitschriftenartikel
132 (2), S. 567 - 575 (2010)
Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase. Journal of the American Chemical Society
Zeitschriftenartikel
49 (44), S. 8112 - 8115 (2010)
Intermediates in the catalytic cycle of methyl coenzyme M reductase: Isotope exchange is consistent with formation of a σ-alkane-nickel complex. Angewandte Chemie International Edition
Zeitschriftenartikel
13 (8), S. 1275 - 1289 (2008)
Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase. Journal of Biological Inorganic Chemistry
Zeitschriftenartikel
130 (33), S. 10907 - 10920 (2008)
A nickel hydride complex in the active site of methyl-coenzyme M reductase: Implications for the catalytic cycle. Journal of the American Chemical Society
Zeitschriftenartikel
12 (8), S. 1097 - 1105 (2007)
Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy. Journal of Biological Inorganic Chemistry
Zeitschriftenartikel
45, S. 3602 - 07 (2006)
A nickel-alkyl bond in an inactivated state of the enzyme catalyzing methane formation. Angewandte Chemie, International Edition in English
Zeitschriftenartikel
127 (50), S. 17744 - 17755 (2005)
Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: A pulse EPR study. Journal of the American Chemical Society
Zeitschriftenartikel
184 (1), S. 41 - 48 (2005)
Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis. Archives of Microbiology
Zeitschriftenartikel
184 (1), S. 41 - 48 (2005)
Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis. Archives of Microbiology
Zeitschriftenartikel
10 (4), S. 333 - 342 (2005)
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B. Journal of Biological Inorganic Chemistry
Zeitschriftenartikel
280 (14), S. 13712 - 13719 (2005)
How an enzyme binds the C-1 carrier tetrahydromethanopterin - Structure of the tetrahydromethanopterin-dependent formaldehyde-aactivating enzyme (Fae) from Methylobacterium extorquens AM1. Journal of Biological Chemistry
Zeitschriftenartikel
9 (6), S. 691 - 705 (2004)
Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues. Journal of Biological Inorganic Chemistry
Zeitschriftenartikel
9 (5), S. 563 - 576 (2004)
Spectroscopic investigation of the nickel-containing porphinoid cofactor F430. 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. Journal of Biological Inorganic Chemistry
Zeitschriftenartikel
125 (17), S. 4988 - 4989 (2003)
Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M reductase. Journal of the American Chemical Society