Kinetic analysis of manganese peroxidase. The reaction with manganese complexes.
Identifieur interne : 000E09 ( Main/Exploration ); précédent : 000E08; suivant : 000E10Kinetic analysis of manganese peroxidase. The reaction with manganese complexes.
Auteurs : I C Kuan [États-Unis] ; K A Johnson ; M. TienSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1993.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Acides carboxyliques, Chélateurs, Manganèse, Peroxidases.
- Cinétique, Liaison aux protéines, Mathématiques, Modèles théoriques.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Carboxylic Acids, Chelating Agents, Manganese, Peroxidases.
- enzymology : Basidiomycota.
- Kinetics, Mathematics, Models, Theoretical, Protein Binding.
Abstract
Manganese peroxidase from the lignin-degrading fungus Phanerochaete chrysosporium catalyzes the H2O2-dependent oxidation of Mn2+ to Mn3+. Presteady-state methods were employed to characterize the reactions of free and chelated Mn2+ with the 2-electron and 1-electron oxidized forms of the enzyme, compounds I and II, respectively. At pH 4.5, the optimum pH for steady-state turnover, the reaction of compound I with Mn2+, either free or complexed, is too rapid to measure by stopped flow methods. The reactions of compound I with Mn2+ can only be monitored under non-optimal conditions of pH 2.5. The reaction of compound II with Mn2+ is much slower than compound I. Chelators such as oxalate, lactate, and malonate facilitated the reaction of Mn2+ with compound II. In contrast, succinate, which does not readily form a complex with Mn2+, and polyglutamate, which is polymeric, were ineffective in stimulating the reaction of Mn2+ with compound II. The 1:1 chelator-Mn2+ complex is the preferred substrate for compound II; this conclusion is based on known formation constants for the various Mn2+ complexes. Steady-state kinetics studies were performed by directly measuring the initial rate of Mn3+ formation. The kcat values for the formation of Mn(3+)-oxalate, Mn(3+)-lactate, and Mn(3+)-malonate are 308, 211, and 220 s-1, respectively. The Km values for Mn(2+)-oxalate, Mn(2+)-lactate, and Mn(2+)-malonate are 13, 41, and 18 microM, respectively. These results collectively indicate that manganese peroxidase does not readily oxidize free (hexa-aquo) Mn2+ as previously proposed (Wariishi, H., Valli, K., and Gold, M. H. (1992) J. Biol. Chem. 267, 23688-23695), but the Mn2+ has to be chelated to support steady-state turnover.
PubMed: 8376363
Affiliations:
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Tien</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8376363</idno><idno type="pmid">8376363</idno><idno type="wicri:Area/Main/Corpus">000D86</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D86</idno><idno type="wicri:Area/Main/Curation">000D86</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D86</idno><idno type="wicri:Area/Main/Exploration">000D86</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Kinetic analysis of manganese peroxidase. The reaction with manganese complexes.</title><author><name sortKey="Kuan, I C" sort="Kuan, I C" uniqKey="Kuan I" first="I C" last="Kuan">I C Kuan</name><affiliation wicri:level="4"><nlm:affiliation>Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.</nlm:affiliation><orgName type="university">Université d'État de Pennsylvanie</orgName><country>États-Unis</country><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Johnson, K A" sort="Johnson, K A" uniqKey="Johnson K" first="K A" last="Johnson">K A Johnson</name></author><author><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Carboxylic Acids (metabolism)</term><term>Chelating Agents (metabolism)</term><term>Kinetics (MeSH)</term><term>Manganese (metabolism)</term><term>Mathematics (MeSH)</term><term>Models, Theoretical (MeSH)</term><term>Peroxidases (metabolism)</term><term>Protein Binding (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides carboxyliques (métabolisme)</term><term>Basidiomycota (enzymologie)</term><term>Chélateurs (métabolisme)</term><term>Cinétique (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Manganèse (métabolisme)</term><term>Mathématiques (MeSH)</term><term>Modèles théoriques (MeSH)</term><term>Peroxidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxylic Acids</term><term>Chelating Agents</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>Acides carboxyliques</term><term>Chélateurs</term><term>Manganèse</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term><term>Mathematics</term><term>Models, Theoretical</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Liaison aux protéines</term><term>Mathématiques</term><term>Modèles théoriques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Manganese peroxidase from the lignin-degrading fungus Phanerochaete chrysosporium catalyzes the H2O2-dependent oxidation of Mn2+ to Mn3+. Presteady-state methods were employed to characterize the reactions of free and chelated Mn2+ with the 2-electron and 1-electron oxidized forms of the enzyme, compounds I and II, respectively. At pH 4.5, the optimum pH for steady-state turnover, the reaction of compound I with Mn2+, either free or complexed, is too rapid to measure by stopped flow methods. The reactions of compound I with Mn2+ can only be monitored under non-optimal conditions of pH 2.5. The reaction of compound II with Mn2+ is much slower than compound I. Chelators such as oxalate, lactate, and malonate facilitated the reaction of Mn2+ with compound II. In contrast, succinate, which does not readily form a complex with Mn2+, and polyglutamate, which is polymeric, were ineffective in stimulating the reaction of Mn2+ with compound II. The 1:1 chelator-Mn2+ complex is the preferred substrate for compound II; this conclusion is based on known formation constants for the various Mn2+ complexes. Steady-state kinetics studies were performed by directly measuring the initial rate of Mn3+ formation. The kcat values for the formation of Mn(3+)-oxalate, Mn(3+)-lactate, and Mn(3+)-malonate are 308, 211, and 220 s-1, respectively. The Km values for Mn(2+)-oxalate, Mn(2+)-lactate, and Mn(2+)-malonate are 13, 41, and 18 microM, respectively. These results collectively indicate that manganese peroxidase does not readily oxidize free (hexa-aquo) Mn2+ as previously proposed (Wariishi, H., Valli, K., and Gold, M. H. (1992) J. Biol. Chem. 267, 23688-23695), but the Mn2+ has to be chelated to support steady-state turnover.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8376363</PMID><DateCompleted><Year>1993</Year><Month>10</Month><Day>20</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>268</Volume><Issue>27</Issue><PubDate><Year>1993</Year><Month>Sep</Month><Day>25</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Kinetic analysis of manganese peroxidase. The reaction with manganese complexes.</ArticleTitle><Pagination><MedlinePgn>20064-70</MedlinePgn></Pagination><Abstract><AbstractText>Manganese peroxidase from the lignin-degrading fungus Phanerochaete chrysosporium catalyzes the H2O2-dependent oxidation of Mn2+ to Mn3+. Presteady-state methods were employed to characterize the reactions of free and chelated Mn2+ with the 2-electron and 1-electron oxidized forms of the enzyme, compounds I and II, respectively. At pH 4.5, the optimum pH for steady-state turnover, the reaction of compound I with Mn2+, either free or complexed, is too rapid to measure by stopped flow methods. The reactions of compound I with Mn2+ can only be monitored under non-optimal conditions of pH 2.5. The reaction of compound II with Mn2+ is much slower than compound I. Chelators such as oxalate, lactate, and malonate facilitated the reaction of Mn2+ with compound II. In contrast, succinate, which does not readily form a complex with Mn2+, and polyglutamate, which is polymeric, were ineffective in stimulating the reaction of Mn2+ with compound II. The 1:1 chelator-Mn2+ complex is the preferred substrate for compound II; this conclusion is based on known formation constants for the various Mn2+ complexes. Steady-state kinetics studies were performed by directly measuring the initial rate of Mn3+ formation. The kcat values for the formation of Mn(3+)-oxalate, Mn(3+)-lactate, and Mn(3+)-malonate are 308, 211, and 220 s-1, respectively. The Km values for Mn(2+)-oxalate, Mn(2+)-lactate, and Mn(2+)-malonate are 13, 41, and 18 microM, respectively. These results collectively indicate that manganese peroxidase does not readily oxidize free (hexa-aquo) Mn2+ as previously proposed (Wariishi, H., Valli, K., and Gold, M. H. (1992) J. Biol. Chem. 267, 23688-23695), but the Mn2+ has to be chelated to support steady-state turnover.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kuan</LastName><ForeName>I C</ForeName><Initials>IC</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>K A</ForeName><Initials>KA</Initials></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1-P42ES04922-01</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, 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="D002264">Carboxylic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002614">Chelating Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002264" MajorTopicYN="N">Carboxylic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002614" MajorTopicYN="N">Chelating Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></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="D008962" MajorTopicYN="N">Models, Theoretical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>9</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>9</Month><Day>25</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>9</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8376363</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region><settlement><li>University Park (Pennsylvanie)</li></settlement><orgName><li>Université d'État de Pennsylvanie</li></orgName></list><tree><noCountry><name sortKey="Johnson, K A" sort="Johnson, K A" uniqKey="Johnson K" first="K A" last="Johnson">K A Johnson</name><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Kuan, I C" sort="Kuan, I C" uniqKey="Kuan I" first="I C" last="Kuan">I C Kuan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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