Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.
Identifieur interne : 000C21 ( Main/Curation ); précédent : 000C20; suivant : 000C22Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.
Auteurs : M. Tatarko [États-Unis] ; J A BumpusSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1997.
Descripteurs français
- KwdFr :
- Analyse spectrale (MeSH), Azotures (composition chimique), Azotures (pharmacologie), Basidiomycota (enzymologie), Composés du fer II (composition chimique), Composés du fer III (composition chimique), Hème (composition chimique), Oxydoréduction (MeSH), Peroxidases (antagonistes et inhibiteurs), Peroxidases (composition chimique), Peroxyde d'hydrogène (composition chimique), Protoxyde d'azote (composition chimique), Protoxyde d'azote (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Peroxidases.
- composition chimique : Azotures, Composés du fer II, Composés du fer III, Hème, Peroxidases, Peroxyde d'hydrogène, Protoxyde d'azote.
- enzymologie : Basidiomycota.
- métabolisme : Protoxyde d'azote.
- pharmacologie : Azotures.
- Analyse spectrale, Oxydoréduction.
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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Tatarko</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences, University of Notre Dame, Indiana 46556, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, University of Notre Dame, Indiana 46556</wicri:regionArea></affiliation></author><author><name sortKey="Bumpus, J A" sort="Bumpus, J A" uniqKey="Bumpus J" first="J A" last="Bumpus">J A Bumpus</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><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><term>Peroxidases (chemistry)</term><term>Spectrum Analysis (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale (MeSH)</term><term>Azotures (composition chimique)</term><term>Azotures (pharmacologie)</term><term>Basidiomycota (enzymologie)</term><term>Composés du fer II (composition chimique)</term><term>Composés du fer III (composition chimique)</term><term>Hème (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (antagonistes et inhibiteurs)</term><term>Peroxidases (composition chimique)</term><term>Peroxyde d'hydrogène (composition chimique)</term><term>Protoxyde d'azote (composition chimique)</term><term>Protoxyde d'azote (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Azides</term><term>Ferric Compounds</term><term>Ferrous Compounds</term><term>Heme</term><term>Hydrogen Peroxide</term><term>Nitrous Oxide</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nitrous Oxide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Azides</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Azotures</term><term>Composés du fer II</term><term>Composés du fer III</term><term>Hème</term><term>Peroxidases</term><term>Peroxyde d'hydrogène</term><term>Protoxyde d'azote</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protoxyde d'azote</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Azotures</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Oxidation-Reduction</term><term>Spectrum Analysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9056250</PMID><DateCompleted><Year>1997</Year><Month>04</Month><Day>16</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>339</Volume><Issue>1</Issue><PubDate><Year>1997</Year><Month>Mar</Month><Day>01</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>200-9</MedlinePgn></Pagination><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></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tatarko</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, University of Notre Dame, Indiana 46556, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bumpus</LastName><ForeName>J A</ForeName><Initials>JA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ESO4922</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001386">Azides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005290">Ferric Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005296">Ferrous Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K50XQU1029</RegistryNumber><NameOfSubstance UI="D009609">Nitrous Oxide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Arch Biochem Biophys 1998 Jan 1;349(1):204</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D001386" MajorTopicYN="N">Azides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005290" MajorTopicYN="N">Ferric Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005296" MajorTopicYN="N">Ferrous Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009609" MajorTopicYN="N">Nitrous Oxide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013057" MajorTopicYN="N">Spectrum Analysis</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>3</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9056250</ArticleId><ArticleId IdType="pii">S0003-9861(96)99839-2</ArticleId><ArticleId IdType="doi">10.1006/abbi.1996.9839</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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