Publikationen von Meike Goenrich

Zeitschriftenartikel (22)

Zeitschriftenartikel
Scheller, S.; Goenrich, M.; Thauer, R. K.; Jaun, B.: 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 135 (40), S. 14985 - 14995 (2013)
Zeitschriftenartikel
Scheller, S.; Goenrich, M.; Thauer, R. K.; Jaun, B.: Methyl-coenzyme M reductase from Methanogenic archaea: Isotope effects on the formation and anaerobic oxidation of methane. Journal of the American Chemical Society 135 (40), S. 14975 - 14984 (2013)
Zeitschriftenartikel
Poehlein, A.; Schmidt, S.; Kaster, A. K.; Goenrich, M.; Vollmers, J.; Thurmer, A.; Bertsch, J.; Schuchmann, K.; Voigt, B.; Hecker, M. et al.; Daniel, R.; Thauer, R. K.; Gottschalk, G.; Muller, V.: An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis. PLOS ONE 7 (3), e33439 (2012)
Zeitschriftenartikel
Kaster, A. K.; Goenrich, M.; Seedorf, H.; Liesegang, H.; Wollherr, A.; Gottschalk, G.; Thauer, R. K.: 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
Liesegang, H.; Kaster, A. K.; Wiezer, A.; Goenrich, M.; Wollherr, A.; Seedorf, H.; Gottschalk, G.; Thauer, R. K.: Complete genome sequence of Methanothermobacter marburgensis, a Methanoarchaeon model organism. Journal of Bacteriology 192 (21), S. 5850 - 5851 (2010)
Zeitschriftenartikel
Scheller, S.; Goenrich, M.; Boecher, R.; Thauer, R. K.; Jaun, B.: The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane. Nature 465 (7298), S. 606 - U97 (2010)
Zeitschriftenartikel
Ebner, S.; Jaun, B.; Goenrich, M.; Thauer, R. K.; Harmer, J.: Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase. Journal of the American Chemical Society 132 (2), S. 567 - 575 (2010)
Zeitschriftenartikel
Scheller, S.; Goenrich, M.; Mayr, S.; Thauer, R. K.; Jaun, B.: 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 49 (44), S. 8112 - 8115 (2010)
Zeitschriftenartikel
Hinderberger, D.; Ebner, S.; Mayr, S.; Jaun, B.; Reiher, M.; Goenrich, M.; Thauer, R. K.; Harmer, J.: Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase. Journal of Biological Inorganic Chemistry 13 (8), S. 1275 - 1289 (2008)
Zeitschriftenartikel
Harmer, J.; Finazzo, C.; Piskorski, R.; Ebner, S.; Duin, E. C.; Goenrich, M.; Thauer, R. K.; Reiher, M.; Schweiger, A.; Hinderberger, D. et al.; Jaun, B.: A nickel hydride complex in the active site of methyl-coenzyme M reductase: Implications for the catalytic cycle. Journal of the American Chemical Society 130 (33), S. 10907 - 10920 (2008)
Zeitschriftenartikel
Kern, D. I.; Goenrich, M.; Jaun, B.; Thauer, R. K.; Harmer, J.; Hinderberger, D.: Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy. Journal of Biological Inorganic Chemistry 12 (8), S. 1097 - 1105 (2007)
Zeitschriftenartikel
Hinderberger, D.; Piskorski, R.; Goenrich, M.; Thauer, R. K.; Schweiger, A.; Harmer, J.; Jaun, B.: A nickel-alkyl bond in an inactivated state of the enzyme catalyzing methane formation. Angewandte Chemie, International Edition in English 45, S. 3602 - 07 (2006)
Zeitschriftenartikel
Harmer, J.; Finazzo, C.; Piskorski, R.; Bauer, C.; Jaun, B.; Duin, E. C.; Goenrich, M.; Thauer, R. K.; Van Doorslaer, S.; Schweiger, A.: 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 127 (50), S. 17744 - 17755 (2005)
Zeitschriftenartikel
Goenrich, M.; Thauer, R. K.; Yurimoto, H.; Kato, N.: Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis. Archives of Microbiology 184 (1), S. 41 - 48 (2005)
Zeitschriftenartikel
Goenrich, M.; Thauer, R. K.; Yurimoto, H.; Kato, N.: Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis. Archives of Microbiology 184 (1), S. 41 - 48 (2005)
Zeitschriftenartikel
Goenrich, M.; Duin, E. C.; Mahlert, F.; Thauer, R. K.: 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 10 (4), S. 333 - 342 (2005)
Zeitschriftenartikel
Acharya, P.; Goenrich, M.; Hagemeier, C. H.; Demmer, U.; Vorholt, J. A.; Thauer, R. K.; Ermler, U.: 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 280 (14), S. 13712 - 13719 (2005)
Zeitschriftenartikel
Goenrich, M.; Mahlert, F.; Duin, E. C.; Bauer, C.; Jaun, B.; Thauer, R. K.: Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues. Journal of Biological Inorganic Chemistry 9 (6), S. 691 - 705 (2004)
Zeitschriftenartikel
Duin, E. C.; Signor, L.; Piskorski, R.; Mahlert, F.; Clay, M. D.; Goenrich, M.; Thauer, R. K.; Jaun, B.; Johnson, M. K.: 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 9 (5), S. 563 - 576 (2004)
Zeitschriftenartikel
Finazzo, C.; Harmer, J.; Bauer, C.; Jaun, B.; Duin, E. C.; Mahlert, F.; Goenrich, M.; Thauer, R. K.; Van Doorslaer, S.; Schweiger, A.: 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 125 (17), S. 4988 - 4989 (2003)
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