Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.
Identifieur interne : 000E62 ( Main/Exploration ); précédent : 000E61; suivant : 000E63Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.
Auteurs : H. Wariishi ; K. Valli ; M H GoldSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1992.
Descripteurs français
- KwdFr :
- Acides carboxyliques (pharmacologie), Alcools benzyliques (métabolisme), Alcools benzyliques (pharmacologie), Basidiomycota (enzymologie), Chélateurs (pharmacologie), Cinétique (MeSH), Lactates (métabolisme), Lactates (pharmacologie), Malonates (métabolisme), Manganèse (métabolisme), Mathématiques (MeSH), Oxydoréduction (MeSH), Peroxidases (métabolisme), Peroxyde d'hydrogène (métabolisme).
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Alcools benzyliques, Lactates, Malonates, Manganèse, Peroxidases, Peroxyde d'hydrogène.
- pharmacologie : Acides carboxyliques, Alcools benzyliques, Chélateurs, Lactates.
- Cinétique, Mathématiques, Oxydoréduction.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Benzyl Alcohols (metabolism), Benzyl Alcohols (pharmacology), Carboxylic Acids (pharmacology), Chelating Agents (pharmacology), Hydrogen Peroxide (metabolism), Kinetics (MeSH), Lactates (metabolism), Lactates (pharmacology), Malonates (metabolism), Manganese (metabolism), Mathematics (MeSH), Oxidation-Reduction (MeSH), Peroxidases (metabolism).
- MESH :
- chemical , metabolism : Benzyl Alcohols, Hydrogen Peroxide, Lactates, Malonates, Manganese, Peroxidases.
- enzymology : Basidiomycota.
- chemical , pharmacology : Benzyl Alcohols, Carboxylic Acids, Chelating Agents, Lactates.
- Kinetics, Mathematics, Oxidation-Reduction.
Abstract
Manganese oxidation by manganese peroxidase (MnP) was investigated. Stoichiometric, kinetic, and MnII binding studies demonstrated that MnP has a single manganese binding site near the heme, and two MnIII equivalents are formed at the expense of one H2O2 equivalent. Since each catalytic cycle step is irreversible, the data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping-pong mechanism. MnIII-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction. MnIII-lactate and -tartrate also react slowly with H2O2, with third-order kinetics. The latter slow reaction does not interfere with the rapid MnP oxidation of phenols. Oxalate and malonate are the only organic acid chelators secreted by the fungus in significant amounts. No relationship between stimulation of enzyme activity and chelator size was found, suggesting that the substrate is free MnII rather than a MnII-chelator complex. The enzyme competes with chelators for free MnII. Optimal chelators, such as malonate, facilitate MnIII dissociation from the enzyme, stabilize MnIII in aqueous solution, and have a relatively low MnII binding constant.
PubMed: 1429709
Affiliations:
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Valli</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:1429709</idno><idno type="pmid">1429709</idno><idno type="wicri:Area/Main/Corpus">000E42</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E42</idno><idno type="wicri:Area/Main/Curation">000E42</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000E42</idno><idno type="wicri:Area/Main/Exploration">000E42</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.</title><author><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name><affiliation><nlm:affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton 97006-1999.</nlm:affiliation><wicri:noCountry code="subField">Beaverton 97006-1999</wicri:noCountry></affiliation></author><author><name sortKey="Valli, K" sort="Valli, K" uniqKey="Valli K" first="K" last="Valli">K. Valli</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Benzyl Alcohols (metabolism)</term><term>Benzyl Alcohols (pharmacology)</term><term>Carboxylic Acids (pharmacology)</term><term>Chelating Agents (pharmacology)</term><term>Hydrogen Peroxide (metabolism)</term><term>Kinetics (MeSH)</term><term>Lactates (metabolism)</term><term>Lactates (pharmacology)</term><term>Malonates (metabolism)</term><term>Manganese (metabolism)</term><term>Mathematics (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides carboxyliques (pharmacologie)</term><term>Alcools benzyliques (métabolisme)</term><term>Alcools benzyliques (pharmacologie)</term><term>Basidiomycota (enzymologie)</term><term>Chélateurs (pharmacologie)</term><term>Cinétique (MeSH)</term><term>Lactates (métabolisme)</term><term>Lactates (pharmacologie)</term><term>Malonates (métabolisme)</term><term>Manganèse (métabolisme)</term><term>Mathématiques (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (métabolisme)</term><term>Peroxyde d'hydrogène (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Hydrogen Peroxide</term><term>Lactates</term><term>Malonates</term><term>Manganese</term><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>Alcools benzyliques</term><term>Lactates</term><term>Malonates</term><term>Manganèse</term><term>Peroxidases</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acides carboxyliques</term><term>Alcools benzyliques</term><term>Chélateurs</term><term>Lactates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Benzyl Alcohols</term><term>Carboxylic Acids</term><term>Chelating Agents</term><term>Lactates</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term><term>Mathematics</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Mathématiques</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Manganese oxidation by manganese peroxidase (MnP) was investigated. Stoichiometric, kinetic, and MnII binding studies demonstrated that MnP has a single manganese binding site near the heme, and two MnIII equivalents are formed at the expense of one H2O2 equivalent. Since each catalytic cycle step is irreversible, the data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping-pong mechanism. MnIII-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction. MnIII-lactate and -tartrate also react slowly with H2O2, with third-order kinetics. The latter slow reaction does not interfere with the rapid MnP oxidation of phenols. Oxalate and malonate are the only organic acid chelators secreted by the fungus in significant amounts. No relationship between stimulation of enzyme activity and chelator size was found, suggesting that the substrate is free MnII rather than a MnII-chelator complex. The enzyme competes with chelators for free MnII. Optimal chelators, such as malonate, facilitate MnIII dissociation from the enzyme, stabilize MnIII in aqueous solution, and have a relatively low MnII binding constant.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1429709</PMID><DateCompleted><Year>1992</Year><Month>12</Month><Day>22</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>267</Volume><Issue>33</Issue><PubDate><Year>1992</Year><Month>Nov</Month><Day>25</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.</ArticleTitle><Pagination><MedlinePgn>23688-95</MedlinePgn></Pagination><Abstract><AbstractText>Manganese oxidation by manganese peroxidase (MnP) was investigated. Stoichiometric, kinetic, and MnII binding studies demonstrated that MnP has a single manganese binding site near the heme, and two MnIII equivalents are formed at the expense of one H2O2 equivalent. Since each catalytic cycle step is irreversible, the data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping-pong mechanism. MnIII-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction. MnIII-lactate and -tartrate also react slowly with H2O2, with third-order kinetics. The latter slow reaction does not interfere with the rapid MnP oxidation of phenols. Oxalate and malonate are the only organic acid chelators secreted by the fungus in significant amounts. No relationship between stimulation of enzyme activity and chelator size was found, suggesting that the substrate is free MnII rather than a MnII-chelator complex. The enzyme competes with chelators for free MnII. Optimal chelators, such as malonate, facilitate MnIII dissociation from the enzyme, stabilize MnIII in aqueous solution, and have a relatively low MnII binding constant.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton 97006-1999.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Valli</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002264">Carboxylic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002614">Chelating Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007773">Lactates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008314">Malonates</NameOfSubstance></Chemical><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</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 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>X7EA1JUA6M</RegistryNumber><NameOfSubstance UI="C024078">vanillyl alcohol</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="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002264" MajorTopicYN="N">Carboxylic Acids</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002614" MajorTopicYN="N">Chelating Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007773" MajorTopicYN="N">Lactates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008314" MajorTopicYN="N">Malonates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008433" MajorTopicYN="N">Mathematics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>11</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>11</Month><Day>25</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>11</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1429709</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name><name sortKey="Valli, K" sort="Valli, K" uniqKey="Valli K" first="K" last="Valli">K. Valli</name><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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