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King Oyster, Eryngii · 2003 · Research Support, Non U.S. Gov'T

High relevance

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

Pleurotus eryngii

SpeciesKing Oyster, Eryngii
JournalJournal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry
Year2003

Key points

  • 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

From the paper

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.

Citation

Banci L, Camarero S, Martínez AT, Martínez MJ, Pérez-Boada M, Pierattelli R, et al. (2003). NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii. Journal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry https://doi.org/10.1007/s00775-003-0476-1 PMID: 12884090

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