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 compar...
| Authors: | , , , , , , |
|---|---|
| Format: | article |
| Status: | Published version |
| Publication Date: | 2003 |
| Country: | España |
| Institution: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repository: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:dnet:digitalcsic_::57b36302a1e29427550df373dc84f3b2 |
| Online Access: | http://hdl.handle.net/10261/429071 https://api.elsevier.com/content/abstract/scopus_id/0141790930 |
| Access Level: | Open access |
| Keyword: | Heme protein Lignin biodegradation Manganese-oxidizing enzyme Site-directed mutagenesis Substrate interaction |
| Summary: | 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. |
|---|