Effect of modified hemes on the spectral properties and activity of manganese peroxidase.
Identifieur interne : 000B79 ( Main/Exploration ); précédent : 000B78; suivant : 000B80Effect of modified hemes on the spectral properties and activity of manganese peroxidase.
Auteurs : N S Reading [États-Unis] ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1998.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Cinétique (MeSH), Composés du fer III (composition chimique), Escherichia coli (génétique), Hème (composition chimique), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (MeSH), Protoporphyrines (composition chimique), Protéines recombinantes (biosynthèse), Protéines recombinantes (isolement et purification), Spectrophotométrie UV (MeSH).
- MESH :
- biosynthèse : Protéines recombinantes.
- composition chimique : Composés du fer III, Hème, Peroxidases, Protoporphyrines.
- génétique : Escherichia coli, Peroxidases.
- isolement et purification : Protéines recombinantes.
- métabolisme : Peroxidases.
- Activation enzymatique, Cinétique, Phanerochaete, Spectrophotométrie UV.
English descriptors
- KwdEn :
- Enzyme Activation (MeSH), Escherichia coli (genetics), Ferric Compounds (chemistry), Heme (chemistry), Kinetics (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (MeSH), Protoporphyrins (chemistry), Recombinant Proteins (biosynthesis), Recombinant Proteins (isolation & purification), Spectrophotometry, Ultraviolet (MeSH).
- MESH :
- chemical , biosynthesis : Recombinant Proteins.
- chemical , chemistry : Ferric Compounds, Heme, Peroxidases, Protoporphyrins.
- genetics : Escherichia coli, Peroxidases.
- chemical , isolation & purification : Recombinant Proteins.
- chemical , metabolism : Peroxidases.
- Enzyme Activation, Kinetics, Phanerochaete, Spectrophotometry, Ultraviolet.
Abstract
Recombinant manganese peroxidase (rMnP), expressed in Escherichia coli as apo-protein, was constituted with Fe(III) protoporphyrin IX, Fe(III) protoporphyrin IX dimethyl ester (DME), Fe(III) deuteroporphyrin (Deut), Fe(III) etioporphyrin III (Etio), and Fe(III) methylpyrrolporphyrin XXI (MPP). The electronic absorption spectra of these hemoproteins were similar to those of native MnP, but absorption maxima were shifted to longer wavelengths in the order of Deut-rMnP, MPP-rMnP, Etio-rMnP, DME-rMnP, and rMnP. All enzymes contained a high-spin, pentacoordinate heme iron as evidenced by the characteristic charge transfer bands in the visible region. The hemoproteins exhibited reduced catalytic activity while maintaining similar substrate Km values compared to native MnP. Compounds I, II, and III were obtained for these hemin-analogue enzymes except for Deut-rMnP. We concluded that the spectral properties of MnP are strongly influenced by porphyrin alpha- and beta-meso edge substituents and manganese oxidation is affected by the gamma-meso edge groups, suggesting a role for the heme propionates in electron transfer during catalysis.
DOI: 10.1006/abbi.1998.0921
PubMed: 9808771
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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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="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Enzyme Activation (MeSH)</term><term>Escherichia coli (genetics)</term><term>Ferric Compounds (chemistry)</term><term>Heme (chemistry)</term><term>Kinetics (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (MeSH)</term><term>Protoporphyrins (chemistry)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (isolation & purification)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term><term>Cinétique (MeSH)</term><term>Composés du fer III (composition chimique)</term><term>Escherichia coli (génétique)</term><term>Hème (composition chimique)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (MeSH)</term><term>Protoporphyrines (composition chimique)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (isolement et purification)</term><term>Spectrophotométrie UV (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ferric Compounds</term><term>Heme</term><term>Peroxidases</term><term>Protoporphyrins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Composés du fer III</term><term>Hème</term><term>Peroxidases</term><term>Protoporphyrines</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Activation</term><term>Kinetics</term><term>Phanerochaete</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Cinétique</term><term>Phanerochaete</term><term>Spectrophotométrie UV</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recombinant manganese peroxidase (rMnP), expressed in Escherichia coli as apo-protein, was constituted with Fe(III) protoporphyrin IX, Fe(III) protoporphyrin IX dimethyl ester (DME), Fe(III) deuteroporphyrin (Deut), Fe(III) etioporphyrin III (Etio), and Fe(III) methylpyrrolporphyrin XXI (MPP). The electronic absorption spectra of these hemoproteins were similar to those of native MnP, but absorption maxima were shifted to longer wavelengths in the order of Deut-rMnP, MPP-rMnP, Etio-rMnP, DME-rMnP, and rMnP. All enzymes contained a high-spin, pentacoordinate heme iron as evidenced by the characteristic charge transfer bands in the visible region. The hemoproteins exhibited reduced catalytic activity while maintaining similar substrate Km values compared to native MnP. Compounds I, II, and III were obtained for these hemin-analogue enzymes except for Deut-rMnP. We concluded that the spectral properties of MnP are strongly influenced by porphyrin alpha- and beta-meso edge substituents and manganese oxidation is affected by the gamma-meso edge groups, suggesting a role for the heme propionates in electron transfer during catalysis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9808771</PMID><DateCompleted><Year>1998</Year><Month>12</Month><Day>22</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>359</Volume><Issue>2</Issue><PubDate><Year>1998</Year><Month>Nov</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Effect of modified hemes on the spectral properties and activity of manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>291-6</MedlinePgn></Pagination><Abstract><AbstractText>Recombinant manganese peroxidase (rMnP), expressed in Escherichia coli as apo-protein, was constituted with Fe(III) protoporphyrin IX, Fe(III) protoporphyrin IX dimethyl ester (DME), Fe(III) deuteroporphyrin (Deut), Fe(III) etioporphyrin III (Etio), and Fe(III) methylpyrrolporphyrin XXI (MPP). The electronic absorption spectra of these hemoproteins were similar to those of native MnP, but absorption maxima were shifted to longer wavelengths in the order of Deut-rMnP, MPP-rMnP, Etio-rMnP, DME-rMnP, and rMnP. All enzymes contained a high-spin, pentacoordinate heme iron as evidenced by the characteristic charge transfer bands in the visible region. The hemoproteins exhibited reduced catalytic activity while maintaining similar substrate Km values compared to native MnP. Compounds I, II, and III were obtained for these hemin-analogue enzymes except for Deut-rMnP. We concluded that the spectral properties of MnP are strongly influenced by porphyrin alpha- and beta-meso edge substituents and manganese oxidation is affected by the gamma-meso edge groups, suggesting a role for the heme propionates in electron transfer during catalysis.</AbstractText><CopyrightInformation>Copyright 1998 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reading</LastName><ForeName>N S</ForeName><Initials>NS</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan, Utah, 84322-4705, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</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="D005290">Ferric Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011524">Protoporphyrins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>C2K325S808</RegistryNumber><NameOfSubstance UI="C028025">protoporphyrin IX</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="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005290" MajorTopicYN="N">Ferric Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011524" MajorTopicYN="N">Protoporphyrins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>11</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>11</Month><Day>11</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>11</Month><Day>11</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9808771</ArticleId><ArticleId IdType="pii">S0003-9861(98)90921-3</ArticleId><ArticleId IdType="doi">10.1006/abbi.1998.0921</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="Reading, N S" sort="Reading, N S" uniqKey="Reading N" first="N S" last="Reading">N S Reading</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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