Effect of calcium on the reversible thermal inactivation of lignin peroxidase.
Identifieur interne : 000C15 ( Main/Exploration ); précédent : 000C14; suivant : 000C16Effect of calcium on the reversible thermal inactivation of lignin peroxidase.
Auteurs : G. Nie [États-Unis] ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1997.
Descripteurs français
- KwdFr :
- MESH :
- antagonistes et inhibiteurs : Peroxidases.
- enzymologie : Basidiomycota.
- métabolisme : Peroxidases.
- pharmacologie : Acide egtazique, Calcium, Oxalates.
- Concentration en ions d'hydrogène, Spectrophotométrie UV, Température élevée.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Peroxidases.
- chemical , metabolism : Peroxidases.
- chemical , pharmacology : Calcium, Egtazic Acid, Oxalates.
- enzymology : Basidiomycota.
- Hot Temperature, Hydrogen-Ion Concentration, Spectrophotometry, Ultraviolet.
Abstract
This study investigated the effects of calcium on the thermal inactivation of lignin peroxidase from Phanerochaete chrysosporium. The monophasic loss of veratryl alcohol oxidase activity corresponded to the loss of calcium when the enzyme was thermally inactivated. Addition of calcium slowed and oxalate and EGTA increased the apparent inactivation rate. The thermally inactivated lignin peroxidase could be readily reactivated by addition of Ca2+. The amount of activity recovered was dependent on temperature, Ca2+ concentration, and incubation conditions. Enzyme activity could be recovered up to 95% of its original value by addition of Ca2+ when lignin peroxidase was depleted of Ca2+ by incubation with EGTA. Although heme absorbance decreased when the enzyme was thermally inactivated, the amount of iron in the enzyme did not change. Changes in the heme environment of the inactivated enzyme were suggested by changes in the electronic absorption in which the Soret band shifted from 408 to 410 nm, the absorption at 502 nm shifted to 532 nm, and the absorption at 634 nm disappeared upon inactivation. Upon the addition of Ca2+, the bands returned to the original wavelength. Therefore, it is proposed that the inactivation mechanism of lignin peroxidase is that the loss of calcium causes heme environmental changes resulting in the loss of enzyme activity.
DOI: 10.1006/abbi.1996.9770
PubMed: 9016817
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Nie</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan 84322-4705</wicri:regionArea><wicri:noRegion>Logan 84322-4705</wicri:noRegion></affiliation></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="1997">1997</date><idno type="RBID">pubmed:9016817</idno><idno type="pmid">9016817</idno><idno type="doi">10.1006/abbi.1996.9770</idno><idno type="wicri:Area/Main/Corpus">000C23</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C23</idno><idno type="wicri:Area/Main/Curation">000C23</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C23</idno><idno type="wicri:Area/Main/Exploration">000C23</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Effect of calcium on the reversible thermal inactivation of lignin peroxidase.</title><author><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. Nie</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan 84322-4705</wicri:regionArea><wicri:noRegion>Logan 84322-4705</wicri:noRegion></affiliation></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="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Calcium (pharmacology)</term><term>Egtazic Acid (pharmacology)</term><term>Hot Temperature (MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Oxalates (pharmacology)</term><term>Peroxidases (antagonists & inhibitors)</term><term>Peroxidases (metabolism)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide egtazique (pharmacologie)</term><term>Basidiomycota (enzymologie)</term><term>Calcium (pharmacologie)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Oxalates (pharmacologie)</term><term>Peroxidases (antagonistes et inhibiteurs)</term><term>Peroxidases (métabolisme)</term><term>Spectrophotométrie UV (MeSH)</term><term>Température élevée (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>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Calcium</term><term>Egtazic Acid</term><term>Oxalates</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Peroxidases</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>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide egtazique</term><term>Calcium</term><term>Oxalates</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hot Temperature</term><term>Hydrogen-Ion Concentration</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Spectrophotométrie UV</term><term>Température élevée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This study investigated the effects of calcium on the thermal inactivation of lignin peroxidase from Phanerochaete chrysosporium. The monophasic loss of veratryl alcohol oxidase activity corresponded to the loss of calcium when the enzyme was thermally inactivated. Addition of calcium slowed and oxalate and EGTA increased the apparent inactivation rate. The thermally inactivated lignin peroxidase could be readily reactivated by addition of Ca2+. The amount of activity recovered was dependent on temperature, Ca2+ concentration, and incubation conditions. Enzyme activity could be recovered up to 95% of its original value by addition of Ca2+ when lignin peroxidase was depleted of Ca2+ by incubation with EGTA. Although heme absorbance decreased when the enzyme was thermally inactivated, the amount of iron in the enzyme did not change. Changes in the heme environment of the inactivated enzyme were suggested by changes in the electronic absorption in which the Soret band shifted from 408 to 410 nm, the absorption at 502 nm shifted to 532 nm, and the absorption at 634 nm disappeared upon inactivation. Upon the addition of Ca2+, the bands returned to the original wavelength. Therefore, it is proposed that the inactivation mechanism of lignin peroxidase is that the loss of calcium causes heme environmental changes resulting in the loss of enzyme activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9016817</PMID><DateCompleted><Year>1997</Year><Month>02</Month><Day>24</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>337</Volume><Issue>2</Issue><PubDate><Year>1997</Year><Month>Jan</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Effect of calcium on the reversible thermal inactivation of lignin peroxidase.</ArticleTitle><Pagination><MedlinePgn>225-31</MedlinePgn></Pagination><Abstract><AbstractText>This study investigated the effects of calcium on the thermal inactivation of lignin peroxidase from Phanerochaete chrysosporium. The monophasic loss of veratryl alcohol oxidase activity corresponded to the loss of calcium when the enzyme was thermally inactivated. Addition of calcium slowed and oxalate and EGTA increased the apparent inactivation rate. The thermally inactivated lignin peroxidase could be readily reactivated by addition of Ca2+. The amount of activity recovered was dependent on temperature, Ca2+ concentration, and incubation conditions. Enzyme activity could be recovered up to 95% of its original value by addition of Ca2+ when lignin peroxidase was depleted of Ca2+ by incubation with EGTA. Although heme absorbance decreased when the enzyme was thermally inactivated, the amount of iron in the enzyme did not change. Changes in the heme environment of the inactivated enzyme were suggested by changes in the electronic absorption in which the Soret band shifted from 408 to 410 nm, the absorption at 502 nm shifted to 532 nm, and the absorption at 634 nm disappeared upon inactivation. Upon the addition of Ca2+, the bands returned to the original wavelength. Therefore, it is proposed that the inactivation mechanism of lignin peroxidase is that the loss of calcium causes heme environmental changes resulting in the loss of enzyme activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nie</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</Affiliation></AffiliationInfo></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="D010070">Oxalates</NameOfSubstance></Chemical><Chemical><RegistryNumber>526U7A2651</RegistryNumber><NameOfSubstance UI="D004533">Egtazic Acid</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>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004533" MajorTopicYN="N">Egtazic Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010070" MajorTopicYN="N">Oxalates</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>1</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>1</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>1</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9016817</ArticleId><ArticleId IdType="pii">S0003-9861(96)99770-2</ArticleId><ArticleId IdType="doi">10.1006/abbi.1996.9770</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. 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