Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase. מאת Ebner, S, Jaun, B, Goenrich, M, Thauer, R, Harmer, J

Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy. מאת Kern, D, Goenrich, M, Jaun, B, Thauer, R, Harmer, J, Hinderberger, D

Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase מאת Hinderberger, D, Ebner, S, Mayr, S, Jaun, B, Reiher, M, Goenrich, M, Thauer, R, Harmer, J

A nickel-alkyl bond in an inactivated state of the enzyme catalyzing methane formation. מאת Hinderberger, D, Piskorski, R, Goenrich, M, Thauer, R, Schweiger, A, Harmer, J, Jaun, B

Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase. מאת Hinderberger, D, Ebner, S, Mayr, S, Jaun, B, Reiher, M, Goenrich, M, Thauer, R, Harmer, J

Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study. מאת Finazzo, C, Harmer, J, Jaun, B, Duin, E, Mahlert, F, Thauer, R, 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. מאת Finazzo, C, Harmer, J, Bauer, C, Jaun, B, Duin, E, Mahlert, F, Goenrich, M, Thauer, R, 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. מאת Harmer, J, Finazzo, C, Piskorski, R, Bauer, C, Jaun, B, Duin, E, Goenrich, M, Thauer, R, Van Doorslaer, S, Schweiger, A

A nickel hydride complex in the active site of methyl-coenzyme m reductase: implications for the catalytic cycle. מאת Harmer, J, Finazzo, C, Piskorski, R, Ebner, S, Duin, E, Goenrich, M, Thauer, R, Reiher, M, Schweiger, A, Hinderberger, D, Jaun, B