B. Jaun

Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy (2007)

Kern, D. I., Goenrich, M., Jaun, B., Thauer, R. K., Harmer, J., Hinderberger, Dariush

NMR-solution structures of fluoro-substituted ß-peptides: A 3 14-helix and a hairpin turn. The first case of a 90° O=C-C-F dihedral angle in an a-fluoro-amide group (2007)

Mathad, R I., Jaun, B., Flogel, O., Gardiner, James, Loweneck, M., Codee, J D. C., ...

To further study the preference of the antiperiplanar (ap) conformation in -fluoro-amide groups, two -peptides, 1 and 2, containing a (2-F)-3hAla and a (2-F)-2hPhe residue, have been synthesized....

NMR-solution structures of fluoro-substituted ß-peptides: A 3 14-helix and a hairpin turn. The first case of a 90° O=C-C-F dihedral angle in an a-fluoro-amide group (2007)

Mathad, R I., Jaun, B., Flogel, O., Gardiner, James, Loweneck, M., Codee, J D. C., ...

To further study the preference of the antiperiplanar (ap) conformation in -fluoro-amide groups, two -peptides, 1 and 2, containing a (2-F)-3hAla and a (2-F)-2hPhe residue, have been synthesized....

Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase. (2005)

Shokes, J. E., Duin, E. C., Bauer, C., Jaun, B., Hedderich, R., Koch, J., ...

Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: A pulse EPR study (2005)

Harmer, J., Finazzo, C., Piskorski, R., Bauer, C., Jaun, B., Duin, E. C., ...

Spectroscopic investigation of the nickel-containing porphinoid cofactor F-430. 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 (2004)

Duin, E. C., Signor, L., Piskorski, R., Mahlert, F., Clay, M. D., Goenrich, M., ...

Methyl-coenzyme M reductase (MCR) catalyzes the methane-forming step in methanogenic archaea. It contains the nickel porphinoid F(430), a prosthetic group that has been proposed to be directly...

Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues (2004)

Goenrich, M., Mahlert, F., Duin, E. C., Bauer, C., Jaun, B., Thauer, R. K.

Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH(3)-S-CoM) with coenzyme B (HS-CoB) to methane and CoM-S-S-CoB. It contains the nickel porphyrinoid F(430) as...

Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study (2003)

Finazzo, C., Harmer, J., Jaun, B., Duin, E. C., Mahlert, F., Thauer, R. K., ...

Methyl-coenzyme M reductase (MCR), which catalyses the reduction of methyl-coenzyme M (CH(3)-S-CoM) with coenzyme B (H-S-CoB) to CH(4) and CoM-S-S-CoB, contains the nickel porphinoid F430 as...

Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F-430 in active methyl-coenzyme M reductase (2003)

Finazzo, C., Harmer, J., Bauer, C., Jaun, B., Duin, E. C., Mahlert, F., ...

Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [S-33]coenzyme M-treated enzyme (2003)

Duin, E. C., Bauer, C., Jaun, B., Hedderich, R.

Heterodisulfide reductase (Hdr) from methanogenic Archaea catalyzes the reversible reduction of the heterodisulfide (CoM-S-S-CoB) of the methanogenic thiol coenzymes, coenzyme M (CoM-SH) and coenzyme...

The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2 (2002)

Mahlert, F., Bauer, C., Jaun, B., Thauer, R. K., Duin, E. C.

Methyl-coenzyme M reductase (MCR) is a nickel enzyme catalyzing the formation of methane from methyl-coenzyme M and coenzyme B in all methanogenic archaea. The active purified enzyme exhibits the...

RNA two-state conformation equilibria and the effect of nucleobase methylation (2002)

Hoebartner, C., Ebert, M. O., Jaun, B., Micura, R.

Methylation of the nucleobases in RNA oligonucleotides mediates duplex–hairpin conversion (2001)

Micura, R., Pils, W., Hoebartner, C., Grubmayr, K., Ebert, M. O., Jaun, B.

Structure of the host-specific toxins produced by the fungal pathogen Periconia circinata.

Macko, V, Stimmel, M B, Wolpert, T J, Dunkle, L D, Acklin, W, Bänteli, R, ...

Four metabolites named peritoxins A and B and periconins A and B have been isolated together with the known metabolite circinatin from culture filtrates of the fungal pathogen Periconia circinata....

Structure of the host-specific toxins produced by the fungal pathogen Periconia circinata.

Macko, V, Stimmel, M B, Wolpert, T J, Dunkle, L D, Acklin, W, Bänteli, R, ...

Four metabolites named peritoxins A and B and periconins A and B have been isolated together with the known metabolite circinatin from culture filtrates of the fungal pathogen Periconia circinata....