Glutathione-mediated transfer of Cu(I) into phytochelatins.
Identifieur interne : 000486 ( Main/Exploration ); précédent : 000485; suivant : 000487Glutathione-mediated transfer of Cu(I) into phytochelatins.
Auteurs : R K Mehra [États-Unis] ; P. MulchandaniSource :
- The Biochemical journal [ 0264-6021 ] ; 1995.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Chromatographie sur gel (MeSH), Cuivre (métabolisme), Données de séquences moléculaires (MeSH), Foie (métabolisme), Glutathion (pharmacologie), Lapins (MeSH), Mesures de luminescence (MeSH), Métalloprotéines (métabolisme), Métallothionéine (métabolisme), Phytochélatines (MeSH), Protéines végétales (métabolisme), Spectrophotométrie UV (MeSH), Stabilité de médicament (MeSH), Séquence d'acides aminés (MeSH), Transport biologique (MeSH).
- MESH :
- métabolisme : Cuivre, Foie, Métalloprotéines, Métallothionéine, Protéines végétales.
- pharmacologie : Glutathion.
- Animaux, Chromatographie sur gel, Données de séquences moléculaires, Lapins, Mesures de luminescence, Phytochélatines, Spectrophotométrie UV, Stabilité de médicament, Séquence d'acides aminés, Transport biologique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Biological Transport (MeSH), Chromatography, Gel (MeSH), Copper (metabolism), Drug Stability (MeSH), Glutathione (pharmacology), Liver (metabolism), Luminescent Measurements (MeSH), Metalloproteins (metabolism), Metallothionein (metabolism), Molecular Sequence Data (MeSH), Phytochelatins (MeSH), Plant Proteins (metabolism), Rabbits (MeSH), Spectrophotometry, Ultraviolet (MeSH).
- MESH :
- chemical , metabolism : Copper, Metalloproteins, Metallothionein, Plant Proteins.
- chemical , pharmacology : Glutathione.
- metabolism : Liver.
- Amino Acid Sequence, Animals, Biological Transport, Chromatography, Gel, Drug Stability, Luminescent Measurements, Molecular Sequence Data, Phytochelatins, Rabbits, Spectrophotometry, Ultraviolet.
Abstract
Room temperature luminescence attributable to Cu(I)-thiolate clusters has been used to probe the transfer of Cu(I) from Cu(I)-glutathione complex to rabbit liver thionein-II and plant metal-binding peptides phytochelatins (gamma-Glu-Cys)2Gly, (gamma-Glu-Cys)3Gly and (gamma-Glu-Cys)4Gly. Reconstitutions were also performed using CuC1. The Cu(I)-binding stoichiometry of metallothionein or phytochelatins was generally independent of the Cu(I) donor. However, the luminescence of the reconstituted metallothionein or phytochelatins was higher when Cu(I)-GSH was the donor. This higher luminescence is presumably due to the stabilizing effect of GSH on Cu(I)-thiolate clusters. As expected, 12 Cu(I) ions were bound per molecule of metallothionein. The Cu(I) binding to phytochelatins depended on their chain length; the binding stoichiometries being 1.25, 2.0 and 2.5 for (gamma-Glu-Cys)2Gly, (gamma-Glu-Cys)3Gly and (gamma-Glu-Cys)4Gly respectively at neutral pH. A reduced stoichiometry for the longer phytochelatins was observed at alkaline pH. No GSH was found to associate with phytochelatins by a gel-filtration assay. The Cu(I) binding to (gamma-Glu-Cys)2Gly and (gamma-Glu-Cys)3Gly occurred in a biphasic manner in the sense that the relative luminescence increased approximately linearly with the amount of Cu(I) up to a certain molar ratio whereafter luminescence increased dramatically upon the binding of additional Cu(I). The luminescence intensity declined once the metal-binding sites were saturated. In analogy with the studies on metallothioneins, biphasic luminescence suggests the formation of two types of Cu(I) clusters in phytochelatins.
DOI: 10.1042/bj3070697
PubMed: 7741699
PubMed Central: PMC1136707
Affiliations:
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Mulchandani</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7741699</idno><idno type="pmid">7741699</idno><idno type="pmc">PMC1136707</idno><idno type="doi">10.1042/bj3070697</idno><idno type="wicri:Area/Main/Corpus">000486</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000486</idno><idno type="wicri:Area/Main/Curation">000486</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000486</idno><idno type="wicri:Area/Main/Exploration">000486</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutathione-mediated transfer of Cu(I) into phytochelatins.</title><author><name sortKey="Mehra, R K" sort="Mehra, R K" uniqKey="Mehra R" first="R K" last="Mehra">R K Mehra</name><affiliation wicri:level="1"><nlm:affiliation>Department of Entomology, University of California, Riverside 92521, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Entomology, University of California, Riverside 92521</wicri:regionArea><wicri:noRegion>Riverside 92521</wicri:noRegion></affiliation></author><author><name sortKey="Mulchandani, P" sort="Mulchandani, P" uniqKey="Mulchandani P" first="P" last="Mulchandani">P. Mulchandani</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Biological Transport (MeSH)</term><term>Chromatography, Gel (MeSH)</term><term>Copper (metabolism)</term><term>Drug Stability (MeSH)</term><term>Glutathione (pharmacology)</term><term>Liver (metabolism)</term><term>Luminescent Measurements (MeSH)</term><term>Metalloproteins (metabolism)</term><term>Metallothionein (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Phytochelatins (MeSH)</term><term>Plant Proteins (metabolism)</term><term>Rabbits (MeSH)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Chromatographie sur gel (MeSH)</term><term>Cuivre (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Foie (métabolisme)</term><term>Glutathion (pharmacologie)</term><term>Lapins (MeSH)</term><term>Mesures de luminescence (MeSH)</term><term>Métalloprotéines (métabolisme)</term><term>Métallothionéine (métabolisme)</term><term>Phytochélatines (MeSH)</term><term>Protéines végétales (métabolisme)</term><term>Spectrophotométrie UV (MeSH)</term><term>Stabilité de médicament (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transport biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term><term>Metalloproteins</term><term>Metallothionein</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cuivre</term><term>Foie</term><term>Métalloprotéines</term><term>Métallothionéine</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Biological Transport</term><term>Chromatography, Gel</term><term>Drug Stability</term><term>Luminescent Measurements</term><term>Molecular Sequence Data</term><term>Phytochelatins</term><term>Rabbits</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chromatographie sur gel</term><term>Données de séquences moléculaires</term><term>Lapins</term><term>Mesures de luminescence</term><term>Phytochélatines</term><term>Spectrophotométrie UV</term><term>Stabilité de médicament</term><term>Séquence d'acides aminés</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Room temperature luminescence attributable to Cu(I)-thiolate clusters has been used to probe the transfer of Cu(I) from Cu(I)-glutathione complex to rabbit liver thionein-II and plant metal-binding peptides phytochelatins (gamma-Glu-Cys)2Gly, (gamma-Glu-Cys)3Gly and (gamma-Glu-Cys)4Gly. Reconstitutions were also performed using CuC1. The Cu(I)-binding stoichiometry of metallothionein or phytochelatins was generally independent of the Cu(I) donor. However, the luminescence of the reconstituted metallothionein or phytochelatins was higher when Cu(I)-GSH was the donor. This higher luminescence is presumably due to the stabilizing effect of GSH on Cu(I)-thiolate clusters. As expected, 12 Cu(I) ions were bound per molecule of metallothionein. The Cu(I) binding to phytochelatins depended on their chain length; the binding stoichiometries being 1.25, 2.0 and 2.5 for (gamma-Glu-Cys)2Gly, (gamma-Glu-Cys)3Gly and (gamma-Glu-Cys)4Gly respectively at neutral pH. A reduced stoichiometry for the longer phytochelatins was observed at alkaline pH. No GSH was found to associate with phytochelatins by a gel-filtration assay. The Cu(I) binding to (gamma-Glu-Cys)2Gly and (gamma-Glu-Cys)3Gly occurred in a biphasic manner in the sense that the relative luminescence increased approximately linearly with the amount of Cu(I) up to a certain molar ratio whereafter luminescence increased dramatically upon the binding of additional Cu(I). The luminescence intensity declined once the metal-binding sites were saturated. In analogy with the studies on metallothioneins, biphasic luminescence suggests the formation of two types of Cu(I) clusters in phytochelatins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7741699</PMID><DateCompleted><Year>1995</Year><Month>06</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>307 ( Pt 3)</Volume><PubDate><Year>1995</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Glutathione-mediated transfer of Cu(I) into phytochelatins.</ArticleTitle><Pagination><MedlinePgn>697-705</MedlinePgn></Pagination><Abstract><AbstractText>Room temperature luminescence attributable to Cu(I)-thiolate clusters has been used to probe the transfer of Cu(I) from Cu(I)-glutathione complex to rabbit liver thionein-II and plant metal-binding peptides phytochelatins (gamma-Glu-Cys)2Gly, (gamma-Glu-Cys)3Gly and (gamma-Glu-Cys)4Gly. Reconstitutions were also performed using CuC1. The Cu(I)-binding stoichiometry of metallothionein or phytochelatins was generally independent of the Cu(I) donor. However, the luminescence of the reconstituted metallothionein or phytochelatins was higher when Cu(I)-GSH was the donor. This higher luminescence is presumably due to the stabilizing effect of GSH on Cu(I)-thiolate clusters. As expected, 12 Cu(I) ions were bound per molecule of metallothionein. The Cu(I) binding to phytochelatins depended on their chain length; the binding stoichiometries being 1.25, 2.0 and 2.5 for (gamma-Glu-Cys)2Gly, (gamma-Glu-Cys)3Gly and (gamma-Glu-Cys)4Gly respectively at neutral pH. A reduced stoichiometry for the longer phytochelatins was observed at alkaline pH. No GSH was found to associate with phytochelatins by a gel-filtration assay. The Cu(I) binding to (gamma-Glu-Cys)2Gly and (gamma-Glu-Cys)3Gly occurred in a biphasic manner in the sense that the relative luminescence increased approximately linearly with the amount of Cu(I) up to a certain molar ratio whereafter luminescence increased dramatically upon the binding of additional Cu(I). The luminescence intensity declined once the metal-binding sites were saturated. In analogy with the studies on metallothioneins, biphasic luminescence suggests the formation of two types of Cu(I) clusters in phytochelatins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mehra</LastName><ForeName>R K</ForeName><Initials>RK</Initials><AffiliationInfo><Affiliation>Department of Entomology, University of California, Riverside 92521, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mulchandani</LastName><ForeName>P</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008667">Metalloproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>9038-94-2</RegistryNumber><NameOfSubstance UI="D008668">Metallothionein</NameOfSubstance></Chemical><Chemical><RegistryNumber>98726-08-0</RegistryNumber><NameOfSubstance UI="D054811">Phytochelatins</NameOfSubstance></Chemical><Chemical><RegistryNumber>C955P95064</RegistryNumber><NameOfSubstance UI="C028419">cuprous chloride</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004355" MajorTopicYN="N">Drug Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008163" MajorTopicYN="N">Luminescent Measurements</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008667" MajorTopicYN="N">Metalloproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008668" MajorTopicYN="N">Metallothionein</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054811" MajorTopicYN="N">Phytochelatins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant 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Mulchandani</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Mehra, R K" sort="Mehra, R K" uniqKey="Mehra R" first="R K" last="Mehra">R K Mehra</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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