Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.
Identifieur interne : 000C21 ( Main/Corpus ); précédent : 000C20; suivant : 000C22Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.
Auteurs : M. Tatarko ; J A BumpusSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1997.
English descriptors
- KwdEn :
- Azides (chemistry), Azides (pharmacology), Basidiomycota (enzymology), Ferric Compounds (chemistry), Ferrous Compounds (chemistry), Heme (chemistry), Hydrogen Peroxide (chemistry), Nitrous Oxide (chemistry), Nitrous Oxide (metabolism), Oxidation-Reduction (MeSH), Peroxidases (antagonists & inhibitors), Peroxidases (chemistry), Spectrum Analysis (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Peroxidases.
- chemical , chemistry : Azides, Ferric Compounds, Ferrous Compounds, Heme, Hydrogen Peroxide, Nitrous Oxide, Peroxidases.
- chemical , metabolism : Nitrous Oxide.
- chemical , pharmacology : Azides.
- enzymology : Basidiomycota.
- Oxidation-Reduction, Spectrum Analysis.
Abstract
Azide ion is a mechanism-based inactivator of horseradish peroxidase [Ortiz de Montellano et al. (1988) Biochemistry 27, 5470-5476] and the peroxidase from the coprophilic fungus Coprinus macrorhizus [DePillis and Ortiz de Montellano (1989) Biochemistry 28, 7947-7952]. These peroxidases mediate the one-electron oxidation of azide ion-forming azidyl radical. Inactivation of these enzymes is caused by covalent modification of the heme prosthetic groups by azidyl radical. Lignin peroxidases from the wood-rotting fungus Phanerochaete chrysosporium are also inactivated when they catalyze oxidation of azide ion [Tuisel et al. (1991) Arch. Biochem. Biophys. 288, 456-462; DePillis et al. (1990) Arch. Biochem. Biophys. 280, 217-223]. Following inactivation of horseradish peroxidase and the peroxidase from C. macrorhizus substantial amounts of azidyl-heme adducts have been found. Only trace amounts of such adducts have been found following azide-mediated inactivation of lignin peroxidase. Nevertheless, we have shown that during oxidation of azide by lignin peroxidase H8 destruction of heme occurred and a substantial fraction of the enzyme is irreversibly inactivated. However, the rest of the enzyme forms a relatively stable ferrous-nitric oxide (NO) complex. Although this complex appears to be an inactivated form of the enzyme, we have shown that, when present as the ferrous-NO complex, the enzyme is actually protected from inactivation. The lignin peroxidase ferrous-NO complex reverts slowly (t1/2 = 6.3 x 10(3) s) to the ferric form. Reversion is accelerated if the complex is chromatographed on a PD-10 (Sephadex G-25) column or if veratryl alcohol is added. If azide and hydrogen peroxide (a required cosubstrate) are present (or added), the enzyme undergoes another cycle of catalysis and further inactivation. A detailed reaction mechanism is proposed that is consistent with our experimental observations, the chemistry of azide, and our current understanding of peroxidases.
DOI: 10.1006/abbi.1996.9839
PubMed: 9056250
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pubmed:9056250Le document en format XML
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<author><name sortKey="Tatarko, M" sort="Tatarko, M" uniqKey="Tatarko M" first="M" last="Tatarko">M. Tatarko</name>
<affiliation><nlm:affiliation>Department of Biological Sciences, University of Notre Dame, Indiana 46556, USA.</nlm:affiliation>
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<author><name sortKey="Bumpus, J A" sort="Bumpus, J A" uniqKey="Bumpus J" first="J A" last="Bumpus">J A Bumpus</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Azides (chemistry)</term>
<term>Azides (pharmacology)</term>
<term>Basidiomycota (enzymology)</term>
<term>Ferric Compounds (chemistry)</term>
<term>Ferrous Compounds (chemistry)</term>
<term>Heme (chemistry)</term>
<term>Hydrogen Peroxide (chemistry)</term>
<term>Nitrous Oxide (chemistry)</term>
<term>Nitrous Oxide (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (antagonists & inhibitors)</term>
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<term>Spectrum Analysis (MeSH)</term>
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<term>Hydrogen Peroxide</term>
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<front><div type="abstract" xml:lang="en">Azide ion is a mechanism-based inactivator of horseradish peroxidase [Ortiz de Montellano et al. (1988) Biochemistry 27, 5470-5476] and the peroxidase from the coprophilic fungus Coprinus macrorhizus [DePillis and Ortiz de Montellano (1989) Biochemistry 28, 7947-7952]. These peroxidases mediate the one-electron oxidation of azide ion-forming azidyl radical. Inactivation of these enzymes is caused by covalent modification of the heme prosthetic groups by azidyl radical. Lignin peroxidases from the wood-rotting fungus Phanerochaete chrysosporium are also inactivated when they catalyze oxidation of azide ion [Tuisel et al. (1991) Arch. Biochem. Biophys. 288, 456-462; DePillis et al. (1990) Arch. Biochem. Biophys. 280, 217-223]. Following inactivation of horseradish peroxidase and the peroxidase from C. macrorhizus substantial amounts of azidyl-heme adducts have been found. Only trace amounts of such adducts have been found following azide-mediated inactivation of lignin peroxidase. Nevertheless, we have shown that during oxidation of azide by lignin peroxidase H8 destruction of heme occurred and a substantial fraction of the enzyme is irreversibly inactivated. However, the rest of the enzyme forms a relatively stable ferrous-nitric oxide (NO) complex. Although this complex appears to be an inactivated form of the enzyme, we have shown that, when present as the ferrous-NO complex, the enzyme is actually protected from inactivation. The lignin peroxidase ferrous-NO complex reverts slowly (t1/2 = 6.3 x 10(3) s) to the ferric form. Reversion is accelerated if the complex is chromatographed on a PD-10 (Sephadex G-25) column or if veratryl alcohol is added. If azide and hydrogen peroxide (a required cosubstrate) are present (or added), the enzyme undergoes another cycle of catalysis and further inactivation. A detailed reaction mechanism is proposed that is consistent with our experimental observations, the chemistry of azide, and our current understanding of peroxidases.</div>
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<Abstract><AbstractText>Azide ion is a mechanism-based inactivator of horseradish peroxidase [Ortiz de Montellano et al. (1988) Biochemistry 27, 5470-5476] and the peroxidase from the coprophilic fungus Coprinus macrorhizus [DePillis and Ortiz de Montellano (1989) Biochemistry 28, 7947-7952]. These peroxidases mediate the one-electron oxidation of azide ion-forming azidyl radical. Inactivation of these enzymes is caused by covalent modification of the heme prosthetic groups by azidyl radical. Lignin peroxidases from the wood-rotting fungus Phanerochaete chrysosporium are also inactivated when they catalyze oxidation of azide ion [Tuisel et al. (1991) Arch. Biochem. Biophys. 288, 456-462; DePillis et al. (1990) Arch. Biochem. Biophys. 280, 217-223]. Following inactivation of horseradish peroxidase and the peroxidase from C. macrorhizus substantial amounts of azidyl-heme adducts have been found. Only trace amounts of such adducts have been found following azide-mediated inactivation of lignin peroxidase. Nevertheless, we have shown that during oxidation of azide by lignin peroxidase H8 destruction of heme occurred and a substantial fraction of the enzyme is irreversibly inactivated. However, the rest of the enzyme forms a relatively stable ferrous-nitric oxide (NO) complex. Although this complex appears to be an inactivated form of the enzyme, we have shown that, when present as the ferrous-NO complex, the enzyme is actually protected from inactivation. The lignin peroxidase ferrous-NO complex reverts slowly (t1/2 = 6.3 x 10(3) s) to the ferric form. Reversion is accelerated if the complex is chromatographed on a PD-10 (Sephadex G-25) column or if veratryl alcohol is added. If azide and hydrogen peroxide (a required cosubstrate) are present (or added), the enzyme undergoes another cycle of catalysis and further inactivation. A detailed reaction mechanism is proposed that is consistent with our experimental observations, the chemistry of azide, and our current understanding of peroxidases.</AbstractText>
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