Oxidation of hydroquinones by the versatile ligninolytic peroxidase fromPleurotus eryngii
نویسندگان
چکیده
منابع مشابه
Bactericidal agents generated by the peroxidase-catalyzed oxidation of para-hydroquinones.
For the three Gram-negative bacteria, Pseudomonas fluorescens, Escherichia coli, and Erwinia amylovora, p-benzoquinone was the principal bactericidal agent formed in vitro during the oxidation of hydroquinone by horseradish peroxidase, whereas no toxicity could be associated with either phenolic or oxygen-free radicals. Even the continuous generation of p-benzosemiquinone during the simultaneou...
متن کاملA new versatile peroxidase from Pleurotus.
Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and li...
متن کاملTwo oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase.
Versatile peroxidase shares with manganese peroxidase and lignin peroxidase the ability to oxidize Mn(2+) and high redox potential aromatic compounds, respectively. Moreover, it is also able to oxidize phenols (and low redox potential dyes) at two catalytic sites, as shown by biphasic kinetics. A high efficiency site (with 2,6-dimethoxyphenol and p-hydroquinone catalytic efficiencies of ∼70 and...
متن کاملEffect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts.
Production of recombinant versatile peroxidase in Aspergillus hosts was optimized through the modification of temperature during bioreactor cultivations. To further this purpose, the cDNA encoding a versatile peroxidase of Pleurotus eryngii was expressed under control of the alcohol dehydrogenase (alcA) promoter of Aspergillus nidulans. A dependence of recombinant peroxidase production on culti...
متن کاملHeterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates.
A versatile ligninolytic peroxidase has been cloned from Pleurotus eryngii and its allelic variant MnPL2 expressed in Aspergillus nidulans, with properties similar to those of the mature enzyme from P. eryngii. These include the ability to oxidize Mn(2+) and aromatic substrates, confirming that this is a new peroxidase type sharing catalytic properties of lignin peroxidase and manganese peroxid...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2001
ISSN: 0014-2956
DOI: 10.1046/j.1432-1327.2001.02405.x