Veratryl alcohol-dependent production of molecular oxygen by lignin peroxidase.
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منابع مشابه
Veratryl alcohol-dependent production of molecular oxygen by lignin peroxidase.
Veratryl alcohol- and H2O2-dependent production of oxygen by lignin peroxidase isozyme H2 (LiPH2) from Phanerochaete chrysosporium was investigated. Veratryl alcohol oxidation by LiPH2 decreased with increasing concentrations of H2O2 while oxygen evolution increased. The absorption spectrum of the LiPH2 in these experiments indicated that it was in the compound II state. We propose that O2 prod...
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Veratryl alcohol (3,4-dimethoxybenzyl alcohol) appears to have multiple roles in lignin degradation by Phanerochaete chrysosporium. It is synthesized de novo by the fungus. It apparently induces expression of lignin peroxidase (LiP), and it protects LiP from inactivation by H2O2. In addition, veratryl alcohol has been shown to potentiate LiP oxidation of compounds that are not good LiP substrat...
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Many white rot fungi are able to produce de novo veratryl alcohol, which is known to be a cofactor involved in the degradation of lignin, lignin model compounds, and xenobiotic pollutants by lignin peroxidase (LiP). In this study, Mn nutrition was shown to strongly influence the endogenous veratryl alcohol levels in the culture fluids of N-deregulated and N-regulated white rot fungi Bjerkandera...
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The mechanism of inhibition of the veratryl alcohol oxidase activity of lignin peroxidase H2 (LiPH2) by EDTA was investigated. It was found that EDTA was decarboxylated and that cytochrome c, nitro blue tetrazolium, ferric iron, and molecular oxygen were reduced in a reaction mixture containing LiPH2, H2O2, veratryl alcohol, and EDTA. The reductive activity observed with LiPH2 followed first or...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)54141-7