| Zitatschlüssel |
Heinfling1998b |
| Autor |
Heinfling, A. and Ruiz-Dueñas, F. J. and Martínez, M. J. and Bergbauer, M. and Szewzyk, U. and Martínez, A. T. |
| Seiten |
141–146 |
| Jahr |
1998 |
| DOI |
doi:10.1016/S0014-5793(98)00512-2 |
| Journal |
FEBS Letters |
| Jahrgang |
428 |
| Nummer |
3 |
| Monat |
May |
| Institution |
FG Microbial Ecology, Technical University of Berlin, Germany. |
| Zusammenfassung |
A novel peroxidase, oxidizing Mn2+ and different aromatic compounds, was isolated. Hydroquinones, substituted phenols, dyes, other aromatic compounds and Mn2+ were compared as reducing substrates, and conclusions presented in the light of a molecular model built by homology modeling. The enzymes showed the fastest reaction rates with Mn2+, but the highest affinity corresponded to hydroquinones and dyes. Oxidation of Reactive Black 5 (an azo-dye not oxidized by Mn3+) was non-competitively inhibited by Mn2+. These findings, together with identification of putative Mn-binding site (involving Glu36, Glu40, Asp175 and inner heme propionate) and long-range electron transfer pathways, indicate that different sites are involved in substrate oxidation. |
