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.
NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii / L. Banci; S. Camarero; A. T. Martinez; M. J. Martinez; M. Perez-Boada; R. Pierattelli; F. J. Ruiz-Duenas. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 8:(2003), pp. 751-760. [10.1007/s00775-003-0476-1]
NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii
BANCI, LUCIA;PIERATTELLI, ROBERTA;
2003
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.
I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
