NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii.
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.
Banci
Lucia
L
Department of Chemistry and Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino (Florence), Italy. banci@cerm.unifi.it
Camarero
Susana
S
Martínez
Angel T
AT
Martínez
María J
MJ
Pérez-Boada
Marta
M
Pierattelli
Roberta
R
Ruiz-Dueñas
Francisco J
FJ
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
D008345:Manganese; D010544:Peroxidases