| Literature DB >> 12884090 |
Lucia Banci1, 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.Entities:
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Year: 2003 PMID: 12884090 DOI: 10.1007/s00775-003-0476-1
Source DB: PubMed Journal: J Biol Inorg Chem ISSN: 0949-8257 Impact factor: 3.358