MetalBindProtPlantV1, Main, Exploration, bibRecord, 000290

Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy.

Identifieur interne : 000290 ( Main/Exploration ); précédent : 000289; suivant : 000291

Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy.

Auteurs : Jordi Domènech [Espagne] ; Anna Tinti ; Mercè Capdevila ; Silvia Atrian ; Armida Torreggiani

Source :

Biopolymers [ 0006-3525 ] ; 2007.

RBID : pubmed:17377964

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Cadmium (metabolism), Histidine (chemistry), Ligands (MeSH), Metallothionein (chemistry), Metallothionein (metabolism), Models, Chemical (MeSH), Molecular Sequence Data (MeSH), Plant Proteins (chemistry), Plant Proteins (metabolism), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Quercus (chemistry), Spectrophotometry, Infrared (MeSH), Spectroscopy, Fourier Transform Infrared (MeSH), Spectrum Analysis (methods), Spectrum Analysis, Raman (MeSH), Stereoisomerism (MeSH), Sulfur (chemistry), Zinc (metabolism).
MESH :
- chemical , chemistry : Histidine, Metallothionein, Plant Proteins, Sulfur.
- chemical , metabolism : Cadmium, Metallothionein, Plant Proteins, Zinc.
- chemistry : Quercus.
- methods : Spectrum Analysis.
- Amino Acid Sequence, Binding Sites, Ligands, Models, Chemical, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Spectrophotometry, Infrared, Spectroscopy, Fourier Transform Infrared, Spectrum Analysis, Raman, Stereoisomerism.

Abstract

Zn- and Cd-complexes of Quercus suber metallothionein (QsMT) were obtained by in vivo-synthesis, in order to obtain physiologically representative aggregates, and characterized by spectrometric and spectroscopic methods. The secondary structure elements and the coordination environments of the metal binding sites of the two aggregates were determined, as well as the main metal-containing species formed. The results obtained from the analysis of the Raman and IR spectra reveal that these metal-MT complexes predominantly contain beta-sheet elements (about 60%), whereas they lack alpha-helices. These structural features slightly depend on the divalent metal bound. In particular, Cd(II) binding to QsMT induces a slight increase of the beta-sheet percentage, as well as a decrease in beta-turn elements with respect to Zn(II) binding. Conversely, the in vivo capability of QsMT to inglobe metal and sulfide ions is metal-depending. Spectroscopic vibrational data also confirm the presence of sulfide ligands in the metal clusters of both Zn- and Cd-QsMT, while the participation of the spacer His residue in metal coordination was only found in Cd-QsMT, in agreement with the CD results. Overall data suggest different coordination environments for Zn(II) and Cd(II) ions in QsMT.

DOI: 10.1002/bip.20729
PubMed: 17377964

Affiliations:

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Le document en format XML

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<author><name sortKey="Domenech, Jordi" sort="Domenech, Jordi" uniqKey="Domenech J" first="Jordi" last="Domènech">Jordi Domènech</name>
<affiliation wicri:level="4"><nlm:affiliation>Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Av. Diagonal 645, 08028 Barcelona (Spain).</nlm:affiliation>
<orgName type="university">Université de Barcelone</orgName>
<country>Espagne</country>
<placeName><settlement type="city">Barcelone</settlement>
<region nuts="2" type="region">Catalogne</region>
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<author><name sortKey="Tinti, Anna" sort="Tinti, Anna" uniqKey="Tinti A" first="Anna" last="Tinti">Anna Tinti</name>
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<author><name sortKey="Capdevila, Merce" sort="Capdevila, Merce" uniqKey="Capdevila M" first="Mercè" last="Capdevila">Mercè Capdevila</name>
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<author><name sortKey="Atrian, Silvia" sort="Atrian, Silvia" uniqKey="Atrian S" first="Silvia" last="Atrian">Silvia Atrian</name>
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<author><name sortKey="Torreggiani, Armida" sort="Torreggiani, Armida" uniqKey="Torreggiani A" first="Armida" last="Torreggiani">Armida Torreggiani</name>
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<affiliation wicri:level="4"><nlm:affiliation>Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Av. Diagonal 645, 08028 Barcelona (Spain).</nlm:affiliation>
<orgName type="university">Université de Barcelone</orgName>
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<author><name sortKey="Tinti, Anna" sort="Tinti, Anna" uniqKey="Tinti A" first="Anna" last="Tinti">Anna Tinti</name>
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<author><name sortKey="Capdevila, Merce" sort="Capdevila, Merce" uniqKey="Capdevila M" first="Mercè" last="Capdevila">Mercè Capdevila</name>
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<author><name sortKey="Atrian, Silvia" sort="Atrian, Silvia" uniqKey="Atrian S" first="Silvia" last="Atrian">Silvia Atrian</name>
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<author><name sortKey="Torreggiani, Armida" sort="Torreggiani, Armida" uniqKey="Torreggiani A" first="Armida" last="Torreggiani">Armida Torreggiani</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Cadmium (metabolism)</term>
<term>Histidine (chemistry)</term>
<term>Ligands (MeSH)</term>
<term>Metallothionein (chemistry)</term>
<term>Metallothionein (metabolism)</term>
<term>Models, Chemical (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Secondary (MeSH)</term>
<term>Quercus (chemistry)</term>
<term>Spectrophotometry, Infrared (MeSH)</term>
<term>Spectroscopy, Fourier Transform Infrared (MeSH)</term>
<term>Spectrum Analysis (methods)</term>
<term>Spectrum Analysis, Raman (MeSH)</term>
<term>Stereoisomerism (MeSH)</term>
<term>Sulfur (chemistry)</term>
<term>Zinc (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale (méthodes)</term>
<term>Analyse spectrale Raman (MeSH)</term>
<term>Cadmium (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Histidine (composition chimique)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Ligands (MeSH)</term>
<term>Modèles chimiques (MeSH)</term>
<term>Métallothionéine (composition chimique)</term>
<term>Métallothionéine (métabolisme)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Quercus (composition chimique)</term>
<term>Sites de fixation (MeSH)</term>
<term>Soufre (composition chimique)</term>
<term>Spectrophotométrie IR (MeSH)</term>
<term>Spectroscopie infrarouge à transformée de Fourier (MeSH)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Stéréoisomérie (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Zinc (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Histidine</term>
<term>Metallothionein</term>
<term>Plant Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cadmium</term>
<term>Metallothionein</term>
<term>Plant Proteins</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Quercus</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Histidine</term>
<term>Métallothionéine</term>
<term>Protéines végétales</term>
<term>Quercus</term>
<term>Soufre</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Spectrum Analysis</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cadmium</term>
<term>Métallothionéine</term>
<term>Protéines végétales</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Analyse spectrale</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Binding Sites</term>
<term>Ligands</term>
<term>Models, Chemical</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Structure, Secondary</term>
<term>Spectrophotometry, Infrared</term>
<term>Spectroscopy, Fourier Transform Infrared</term>
<term>Spectrum Analysis, Raman</term>
<term>Stereoisomerism</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term>
<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Ligands</term>
<term>Modèles chimiques</term>
<term>Sites de fixation</term>
<term>Spectrophotométrie IR</term>
<term>Spectroscopie infrarouge à transformée de Fourier</term>
<term>Structure secondaire des protéines</term>
<term>Stéréoisomérie</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Zn- and Cd-complexes of Quercus suber metallothionein (QsMT) were obtained by in vivo-synthesis, in order to obtain physiologically representative aggregates, and characterized by spectrometric and spectroscopic methods. The secondary structure elements and the coordination environments of the metal binding sites of the two aggregates were determined, as well as the main metal-containing species formed. The results obtained from the analysis of the Raman and IR spectra reveal that these metal-MT complexes predominantly contain beta-sheet elements (about 60%), whereas they lack alpha-helices. These structural features slightly depend on the divalent metal bound. In particular, Cd(II) binding to QsMT induces a slight increase of the beta-sheet percentage, as well as a decrease in beta-turn elements with respect to Zn(II) binding. Conversely, the in vivo capability of QsMT to inglobe metal and sulfide ions is metal-depending. Spectroscopic vibrational data also confirm the presence of sulfide ligands in the metal clusters of both Zn- and Cd-QsMT, while the participation of the spacer His residue in metal coordination was only found in Cd-QsMT, in agreement with the CD results. Overall data suggest different coordination environments for Zn(II) and Cd(II) ions in QsMT.</div>
</front>
</TEI>
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<DateCompleted><Year>2007</Year>
<Month>07</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
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<JournalIssue CitedMedium="Print"><Volume>86</Volume>
<Issue>3</Issue>
<PubDate><Year>2007</Year>
<Month>Jun</Month>
<Day>15</Day>
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<Title>Biopolymers</Title>
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<ArticleTitle>Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy.</ArticleTitle>
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<Abstract><AbstractText>Zn- and Cd-complexes of Quercus suber metallothionein (QsMT) were obtained by in vivo-synthesis, in order to obtain physiologically representative aggregates, and characterized by spectrometric and spectroscopic methods. The secondary structure elements and the coordination environments of the metal binding sites of the two aggregates were determined, as well as the main metal-containing species formed. The results obtained from the analysis of the Raman and IR spectra reveal that these metal-MT complexes predominantly contain beta-sheet elements (about 60%), whereas they lack alpha-helices. These structural features slightly depend on the divalent metal bound. In particular, Cd(II) binding to QsMT induces a slight increase of the beta-sheet percentage, as well as a decrease in beta-turn elements with respect to Zn(II) binding. Conversely, the in vivo capability of QsMT to inglobe metal and sulfide ions is metal-depending. Spectroscopic vibrational data also confirm the presence of sulfide ligands in the metal clusters of both Zn- and Cd-QsMT, while the participation of the spacer His residue in metal coordination was only found in Cd-QsMT, in agreement with the CD results. Overall data suggest different coordination environments for Zn(II) and Cd(II) ions in QsMT.</AbstractText>
<CopyrightInformation>Copyright 2007 Wiley Periodicals, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Domènech</LastName>
<ForeName>Jordi</ForeName>
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<AffiliationInfo><Affiliation>Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Av. Diagonal 645, 08028 Barcelona (Spain).</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tinti</LastName>
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<Initials>A</Initials>
</Author>
<Author ValidYN="Y"><LastName>Capdevila</LastName>
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<Author ValidYN="Y"><LastName>Atrian</LastName>
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<Author ValidYN="Y"><LastName>Torreggiani</LastName>
<ForeName>Armida</ForeName>
<Initials>A</Initials>
</Author>
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<Language>eng</Language>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>00BH33GNGH</RegistryNumber>
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<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
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<MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName>
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	Serveur d'exploration sur les protéines de liaison chez les plantes
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Serveur d'exploration sur les protéines de liaison chez les plantes

Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy.

Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy.

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English descriptors

Abstract

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