title: NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii.
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.
authors.affiliation: Department of Chemistry and Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino (Florence), Italy. banci@cerm.unifi.it
authors.forename: Lucia
authors.initials: L
authors.lastname: Banci
authors.forename: Susana
authors.initials: S
authors.lastname: Camarero
authors.forename: Angel T
authors.initials: AT
authors.lastname: Martínez
authors.forename: María J
authors.initials: MJ
authors.lastname: Martínez
authors.forename: Marta
authors.initials: M
authors.lastname: Pérez-Boada
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Ruiz-Dueñas
mesh_terms: D001665:Binding Sites / Q000235:genetics; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008345:Manganese / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D009154:Mutation; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism; D020076:Pleurotus / Q000201:enzymology*; D011485:Protein Binding
chemical_list: D008345:Manganese; D010544:Peroxidases