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

被引：22

作者：

Banci, L

Camarero, S

Martínez, AT

Martínez, MJ

Pérez-Boada, M

Pierattelli, R

Ruiz-Dueñas, FJ

机构：

[1] Univ Florence, Dept Chem, I-50019 Florence, Italy

[2] Univ Florence, Magnet Resonance Ctr, I-50019 Florence, Italy

[3] CSIC, Ctr Invest Biol, E-28006 Madrid, Spain

来源：

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2003年 / 8卷 / 07期

关键词：

heme protein; lignin biodegradation; manganese-oxidizing enzyme; site-directed mutagenesis; substrate interaction;

D O I：

10.1007/s00775-003-0476-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

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页码：751 / 760

页数：10

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