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- Title
NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii.
- Authors
Lucia Banci; Susana Camarero; Angel T. Martínez; María J. Martínez; Marta Pérez-Boada; Roberta Pierattelli; Francisco J. Ruiz-Dueñas
- Abstract
Nuclear magnetic resonance spectroscopy has been used to characterize the versatile peroxidase from Pleurotus eryngii, both in the resting state and in the cyanide-inhibited form. The assignment of most of the hyperfine-shifted resonances has been achieved by two-dimensional NMR, allowing the comparison of the present system with other ligninolytic peroxidases. This information has enabled a detailed analysis of the interaction of the enzyme with one of its reducing substrates, Mn(II). Furthermore, comparison with the data collected on a mutant in the putative Mn(II) binding site, and an analysis of the enzyme kinetic properties, shed light on the factors affecting the function of this novel peroxidase.
- Subjects
PLEUROTUS; PEROXIDASE; NUCLEAR magnetic resonance; MANGANESE compounds
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2003, Vol 8, Issue 7, p751
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-003-0476-1