Haloperoxidase activity of manganese peroxidase from Phanerochaete chrysosporium.
Identifieur interne : 000C09 ( Main/Exploration ); précédent : 000C08; suivant : 000C10Haloperoxidase activity of manganese peroxidase from Phanerochaete chrysosporium.
Auteurs : D. Sheng [États-Unis] ; M H GoldSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1997.
Descripteurs français
- KwdFr :
- Antienzymes (pharmacologie), Basidiomycota (enzymologie), Bromures (métabolisme), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Iodures (métabolisme), Manganèse (pharmacologie), Oxydoréduction (MeSH), Peroxidases (antagonistes et inhibiteurs), Peroxidases (métabolisme), Peroxyde d'hydrogène (métabolisme), Spectrophotométrie (MeSH).
- MESH :
- antagonistes et inhibiteurs : Peroxidases.
- enzymologie : Basidiomycota.
- métabolisme : Bromures, Iodures, Peroxidases, Peroxyde d'hydrogène.
- pharmacologie : Antienzymes, Manganèse.
- Cinétique, Concentration en ions d'hydrogène, Oxydoréduction, Spectrophotométrie.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Bromides (metabolism), Enzyme Inhibitors (pharmacology), Hydrogen Peroxide (metabolism), Hydrogen-Ion Concentration (MeSH), Iodides (metabolism), Kinetics (MeSH), Manganese (pharmacology), Oxidation-Reduction (MeSH), Peroxidases (antagonists & inhibitors), Peroxidases (metabolism), Spectrophotometry (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Peroxidases.
- chemical , metabolism : Bromides, Hydrogen Peroxide, Iodides, Peroxidases.
- enzymology : Basidiomycota.
- chemical , pharmacology : Enzyme Inhibitors, Manganese.
- Hydrogen-Ion Concentration, Kinetics, Oxidation-Reduction, Spectrophotometry.
Abstract
Manganese peroxidase (MnP) from Phanerochaete chrysosporium exhibits haloperoxidase activity at low pH. In the presence of hydrogen peroxide, MnP oxidizes bromide and iodide as measured by the formation of tribromide and triiodide complexes and the halogenation of various organic substrates. The optimum pHs for bromide and iodide oxidation are 2.5 and 3.0, respectively. Transient-state kinetic studies show that the reaction between MnP compound I and bromide or iodide occurs via a single two-electron step process, obeying second-order kinetics. The second-order rate constants for MnP compound I reduction by bromide and iodide are (4.1 +/- 0.2) x 10(3) and (1.1 +/- 0.1) x 10(5) m-1 s-1, respectively, at pH 3.0. MnP brominates a variety of aromatic substrates, including veratryl (3,4-di-methoxybenzyl) alcohol (I) to produce of 2-bromo-4,5-dimethoxybenzyl alcohol (II). MnP also hydrobrominates cinnamic acid (VI) to produce 2-bromo-3-hydroxyphenylpropionic acid (VII). With 3,4-dimethoxycinnamic acid (III) as the substrate, two bromination products are identified: trans-2-bromo-1-(3, 4-dimethoxyphenyl) ethylene (IV) and 2-bromo-3-(3, 4-dimethoxyphenyl)-3-hydroxypropionic acid (V). MnP also brominates 1,3-dicarbonyl compounds such as monochlorodimedone and malonic acid. Incubation of MnP with bromide and H2O2 in the absence of organic substrates results in enzyme inactivation. MnP binds halides to produce characteristic optical difference spectra. From these spectra, apparent dissociation constants at pH 3.0 are determined to be 0.13, 20, and 45 mm for fluoride, chloride, and bromide, respectively.
DOI: 10.1006/abbi.1997.0217
PubMed: 9281319
Affiliations:
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Sheng</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000</wicri:regionArea><wicri:noRegion>Oregon 97291-1000</wicri:noRegion></affiliation></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="1997">1997</date><idno type="RBID">pubmed:9281319</idno><idno type="pmid">9281319</idno><idno type="doi">10.1006/abbi.1997.0217</idno><idno type="wicri:Area/Main/Corpus">000B99</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B99</idno><idno type="wicri:Area/Main/Curation">000B99</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B99</idno><idno type="wicri:Area/Main/Exploration">000B99</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Haloperoxidase activity of manganese peroxidase from Phanerochaete chrysosporium.</title><author><name sortKey="Sheng, D" sort="Sheng, D" uniqKey="Sheng D" first="D" last="Sheng">D. Sheng</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000</wicri:regionArea><wicri:noRegion>Oregon 97291-1000</wicri:noRegion></affiliation></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">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>Bromides (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Hydrogen Peroxide (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Iodides (metabolism)</term><term>Kinetics (MeSH)</term><term>Manganese (pharmacology)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (antagonists & inhibitors)</term><term>Peroxidases (metabolism)</term><term>Spectrophotometry (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes (pharmacologie)</term><term>Basidiomycota (enzymologie)</term><term>Bromures (métabolisme)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Iodures (métabolisme)</term><term>Manganèse (pharmacologie)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (antagonistes et inhibiteurs)</term><term>Peroxidases (métabolisme)</term><term>Peroxyde d'hydrogène (métabolisme)</term><term>Spectrophotométrie (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>Bromides</term><term>Hydrogen Peroxide</term><term>Iodides</term><term>Peroxidases</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>Bromures</term><term>Iodures</term><term>Peroxidases</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term><term>Manganèse</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Manganese</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Oxidation-Reduction</term><term>Spectrophotometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Oxydoréduction</term><term>Spectrophotométrie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Manganese peroxidase (MnP) from Phanerochaete chrysosporium exhibits haloperoxidase activity at low pH. In the presence of hydrogen peroxide, MnP oxidizes bromide and iodide as measured by the formation of tribromide and triiodide complexes and the halogenation of various organic substrates. The optimum pHs for bromide and iodide oxidation are 2.5 and 3.0, respectively. Transient-state kinetic studies show that the reaction between MnP compound I and bromide or iodide occurs via a single two-electron step process, obeying second-order kinetics. The second-order rate constants for MnP compound I reduction by bromide and iodide are (4.1 +/- 0.2) x 10(3) and (1.1 +/- 0.1) x 10(5) m-1 s-1, respectively, at pH 3.0. MnP brominates a variety of aromatic substrates, including veratryl (3,4-di-methoxybenzyl) alcohol (I) to produce of 2-bromo-4,5-dimethoxybenzyl alcohol (II). MnP also hydrobrominates cinnamic acid (VI) to produce 2-bromo-3-hydroxyphenylpropionic acid (VII). With 3,4-dimethoxycinnamic acid (III) as the substrate, two bromination products are identified: trans-2-bromo-1-(3, 4-dimethoxyphenyl) ethylene (IV) and 2-bromo-3-(3, 4-dimethoxyphenyl)-3-hydroxypropionic acid (V). MnP also brominates 1,3-dicarbonyl compounds such as monochlorodimedone and malonic acid. Incubation of MnP with bromide and H2O2 in the absence of organic substrates results in enzyme inactivation. MnP binds halides to produce characteristic optical difference spectra. From these spectra, apparent dissociation constants at pH 3.0 are determined to be 0.13, 20, and 45 mm for fluoride, chloride, and bromide, respectively.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9281319</PMID><DateCompleted><Year>1997</Year><Month>10</Month><Day>02</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>345</Volume><Issue>1</Issue><PubDate><Year>1997</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Haloperoxidase activity of manganese peroxidase from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>126-34</MedlinePgn></Pagination><Abstract><AbstractText>Manganese peroxidase (MnP) from Phanerochaete chrysosporium exhibits haloperoxidase activity at low pH. In the presence of hydrogen peroxide, MnP oxidizes bromide and iodide as measured by the formation of tribromide and triiodide complexes and the halogenation of various organic substrates. The optimum pHs for bromide and iodide oxidation are 2.5 and 3.0, respectively. Transient-state kinetic studies show that the reaction between MnP compound I and bromide or iodide occurs via a single two-electron step process, obeying second-order kinetics. The second-order rate constants for MnP compound I reduction by bromide and iodide are (4.1 +/- 0.2) x 10(3) and (1.1 +/- 0.1) x 10(5) m-1 s-1, respectively, at pH 3.0. MnP brominates a variety of aromatic substrates, including veratryl (3,4-di-methoxybenzyl) alcohol (I) to produce of 2-bromo-4,5-dimethoxybenzyl alcohol (II). MnP also hydrobrominates cinnamic acid (VI) to produce 2-bromo-3-hydroxyphenylpropionic acid (VII). With 3,4-dimethoxycinnamic acid (III) as the substrate, two bromination products are identified: trans-2-bromo-1-(3, 4-dimethoxyphenyl) ethylene (IV) and 2-bromo-3-(3, 4-dimethoxyphenyl)-3-hydroxypropionic acid (V). MnP also brominates 1,3-dicarbonyl compounds such as monochlorodimedone and malonic acid. Incubation of MnP with bromide and H2O2 in the absence of organic substrates results in enzyme inactivation. MnP binds halides to produce characteristic optical difference spectra. From these spectra, apparent dissociation constants at pH 3.0 are determined to be 0.13, 20, and 45 mm for fluoride, chloride, and bromide, respectively.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sheng</LastName><ForeName>D</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000, USA.</Affiliation></AffiliationInfo></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>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001965">Bromides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007454">Iodides</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001965" MajorTopicYN="N">Bromides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007454" MajorTopicYN="N">Iodides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></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="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9281319</ArticleId><ArticleId IdType="pii">S0003-9861(97)90217-4</ArticleId><ArticleId IdType="doi">10.1006/abbi.1997.0217</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Sheng, D" sort="Sheng, D" uniqKey="Sheng D" first="D" last="Sheng">D. 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