Inhibition of lignin peroxidase H2 by sodium azide.
Identifieur interne : 000F11 ( Main/Corpus ); précédent : 000F10; suivant : 000F12Inhibition of lignin peroxidase H2 by sodium azide.
Auteurs : H. Tuisel ; T A Grover ; J R Lancaster ; J A Bumpus ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1991.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Peroxidases.
- chemical , metabolism : Benzyl Alcohols.
- chemical , pharmacology : Azides.
- enzymology : Agaricales.
- Electron Spin Resonance Spectroscopy, Kinetics, Sodium Azide, Spectrophotometry.
Abstract
The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was strongly inhibited by sodium azide. Inhibition was competitive with respect to veratryl alcohol (Ki = 1-2 microM) and uncompetitive with respect to H2O2. In contrast, sodium azide bound to the native enzyme at pH 6.0 with an apparent dissociation constant (KD) of 126 mM. Formation of azidyl radicals was detected by ESR spin trapping techniques. The enzymes is nearly completely inactivated in four turnovers. The H2O2-activated enzyme intermediate (compound I) reacted with sodium azide to form a new species rather than be reduced to the enzyme intermediate compound II. The new species has absorption maxima at 418, 540, and 570 nm, suggesting the formation of a ferrous-lignin peroxidase-NO complex. Confirmation of this assignment was obtained by low-temperature ESR spectroscopy. An identical complex could be simulated by the addition of nitrite to the reduced enzyme. The enzyme intermediate compound II is readily reduced by sodium azide to native enzyme with essentially no loss of activity.
DOI: 10.1016/0003-9861(91)90220-d
PubMed: 1654834
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pubmed:1654834Le document en format XML
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Tuisel</name><affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4700.</nlm:affiliation></affiliation></author><author><name sortKey="Grover, T A" sort="Grover, T A" uniqKey="Grover T" first="T A" last="Grover">T A Grover</name></author><author><name sortKey="Lancaster, J R" sort="Lancaster, J R" uniqKey="Lancaster J" first="J R" last="Lancaster">J R Lancaster</name></author><author><name sortKey="Bumpus, J A" sort="Bumpus, J A" uniqKey="Bumpus J" first="J A" last="Bumpus">J A Bumpus</name></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1654834</idno><idno type="pmid">1654834</idno><idno type="doi">10.1016/0003-9861(91)90220-d</idno><idno type="wicri:Area/Main/Corpus">000F11</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F11</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibition of lignin peroxidase H2 by sodium azide.</title><author><name sortKey="Tuisel, H" sort="Tuisel, H" uniqKey="Tuisel H" first="H" last="Tuisel">H. Tuisel</name><affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4700.</nlm:affiliation></affiliation></author><author><name sortKey="Grover, T A" sort="Grover, T A" uniqKey="Grover T" first="T A" last="Grover">T A Grover</name></author><author><name sortKey="Lancaster, J R" sort="Lancaster, J R" uniqKey="Lancaster J" first="J R" last="Lancaster">J R Lancaster</name></author><author><name sortKey="Bumpus, J A" sort="Bumpus, J A" uniqKey="Bumpus J" first="J A" last="Bumpus">J A Bumpus</name></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (enzymology)</term><term>Azides (pharmacology)</term><term>Benzyl Alcohols (metabolism)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Kinetics (MeSH)</term><term>Peroxidases (antagonists & inhibitors)</term><term>Sodium Azide (MeSH)</term><term>Spectrophotometry (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Azides</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term><term>Kinetics</term><term>Sodium Azide</term><term>Spectrophotometry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was strongly inhibited by sodium azide. Inhibition was competitive with respect to veratryl alcohol (Ki = 1-2 microM) and uncompetitive with respect to H2O2. In contrast, sodium azide bound to the native enzyme at pH 6.0 with an apparent dissociation constant (KD) of 126 mM. Formation of azidyl radicals was detected by ESR spin trapping techniques. The enzymes is nearly completely inactivated in four turnovers. The H2O2-activated enzyme intermediate (compound I) reacted with sodium azide to form a new species rather than be reduced to the enzyme intermediate compound II. The new species has absorption maxima at 418, 540, and 570 nm, suggesting the formation of a ferrous-lignin peroxidase-NO complex. Confirmation of this assignment was obtained by low-temperature ESR spectroscopy. An identical complex could be simulated by the addition of nitrite to the reduced enzyme. The enzyme intermediate compound II is readily reduced by sodium azide to native enzyme with essentially no loss of activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1654834</PMID><DateCompleted><Year>1991</Year><Month>10</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>288</Volume><Issue>2</Issue><PubDate><Year>1991</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Inhibition of lignin peroxidase H2 by sodium azide.</ArticleTitle><Pagination><MedlinePgn>456-62</MedlinePgn></Pagination><Abstract><AbstractText>The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was strongly inhibited by sodium azide. Inhibition was competitive with respect to veratryl alcohol (Ki = 1-2 microM) and uncompetitive with respect to H2O2. In contrast, sodium azide bound to the native enzyme at pH 6.0 with an apparent dissociation constant (KD) of 126 mM. Formation of azidyl radicals was detected by ESR spin trapping techniques. The enzymes is nearly completely inactivated in four turnovers. The H2O2-activated enzyme intermediate (compound I) reacted with sodium azide to form a new species rather than be reduced to the enzyme intermediate compound II. The new species has absorption maxima at 418, 540, and 570 nm, suggesting the formation of a ferrous-lignin peroxidase-NO complex. Confirmation of this assignment was obtained by low-temperature ESR spectroscopy. An identical complex could be simulated by the addition of nitrite to the reduced enzyme. The enzyme intermediate compound II is readily reduced by sodium azide to native enzyme with essentially no loss of activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tuisel</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan 84322-4700.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grover</LastName><ForeName>T A</ForeName><Initials>TA</Initials></Author><Author ValidYN="Y"><LastName>Lancaster</LastName><ForeName>J R</ForeName><Initials>JR</Initials><Suffix>Jr</Suffix></Author><Author ValidYN="Y"><LastName>Bumpus</LastName><ForeName>J A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ES04922</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="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>968JJ8C9DV</RegistryNumber><NameOfSubstance UI="D019810">Sodium Azide</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>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000363" MajorTopicYN="N">Agaricales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001386" MajorTopicYN="N">Azides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019810" MajorTopicYN="N">Sodium Azide</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>8</Month><Day>11</Day><Hour>19</Hour><Minute>15</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>8</Month><Day>11</Day><Hour>19</Hour><Minute>15</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1654834</ArticleId><ArticleId IdType="pii">0003-9861(91)90220-D</ArticleId><ArticleId IdType="doi">10.1016/0003-9861(91)90220-d</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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