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1: J Biol Inorg Chem. 2003 Sep;8(7):751-60. Epub 2003 Jul 15.Click here to read Links

NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii.

Banci L, Camarero S, Martínez AT, Martínez MJ, Pérez-Boada M, Pierattelli R, Ruiz-Dueñas FJ.

Department of Chemistry and Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino (Florence), Italy. banci@cerm.unifi.it

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.

PMID: 12884090 [PubMed - indexed for MEDLINE]