<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Domenech, Jordi</style></author><author><style face="normal" font="default" size="100%">Orihuela, Ruben</style></author><author><style face="normal" font="default" size="100%">Mir, Gisela</style></author><author><style face="normal" font="default" size="100%">Molinas, Marisa</style></author><author><style face="normal" font="default" size="100%">Atrian, Silvia</style></author><author><style face="normal" font="default" size="100%">Capdevila, Merce</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Cd(II)-binding abilities of recombinant Quercus suber metallothionein: bridging the gap between phytochelatins and metallothioneins.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cadmium</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium–His binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutathione</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolic Detoxication</style></keyword><keyword><style  face="normal" font="default" size="100%">metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">Metallothionein: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Metallothionein: metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Phytochelatins</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins: metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Quercus</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sulfide ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">yeast complementation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2007///</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/17503092</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">867 - 882</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In this work, we have analyzed both at stoichiometric and at conformational level the Cd(II)-binding features of a type 2 plant metallothionein (MT) (the cork oak, Quercus suber, QsMT). To this end four peptides, the wild-type QsMT and three constructs previously engineered to characterize its Zn(II)- and Cu(I)-binding behaviour, were heterologously produced in Escherichia coli cultures supplemented with Cd(II), and the corresponding complexes were purified up to homogeneity. The Cd(II)-binding ability of these recombinant peptides was determined through the chemical, spectroscopic and spectrometric characterization of the recovered clusters. Recombinant synthesis of the four QsMT peptides in cadmium-rich media rendered complexes with a higher metal content than those obtained from zinc-supplemented cultures and, consequently, the recovered Cd(II) species are nonisostructural to those of Zn(II). Also of interest is the fact that three out of the four peptides yielded recombinant preparations that included S(2-)-containing Cd(II) complexes as major species. Subsequently, the in vitro Zn(II)/Cd(II) replacement reactions were studied, as well as the in vitro acid denaturation and S(2-) renaturation reactions. Finally, the capacity of the four peptides for preventing cadmium deleterious effects in yeast cells was tested through complementation assays. Consideration of all the results enables us to suggest a hairpin folding model for this typical type 2 plant Cd(II)-MT complex, as well as a nonnegligible role of the spacer in the detoxification function of QsMT towards cadmium.</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><notes><style face="normal" font="default" size="100%">The following values have no corresponding Zotero field:&lt;br/&gt;accession-num: 17503092</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Domenech, Jordi</style></author><author><style face="normal" font="default" size="100%">Orihuela, Ruben</style></author><author><style face="normal" font="default" size="100%">Mir, Gisela</style></author><author><style face="normal" font="default" size="100%">Molinas, Marisa</style></author><author><style face="normal" font="default" size="100%">Atrian, Silvia</style></author><author><style face="normal" font="default" size="100%">Capdevila, Merce</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Cd(II)-binding abilities of recombinant Quercus suber metallothionein: bridging the gap between phytochelatins and metallothioneins.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cadmium</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium–His binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutathione</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolic Detoxication</style></keyword><keyword><style  face="normal" font="default" size="100%">metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">Metallothionein: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Metallothionein: metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Phytochelatins</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins: metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Quercus</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sulfide ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">yeast complementation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year></dates><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">867-882</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In this work, we have analyzed both at stoichiometric and at conformational level the Cd(II)-binding features of a type 2 plant metallothionein (MT) (the cork oak, Quercus suber, QsMT). To this end four peptides, the wild-type QsMT and three constructs previously engineered to characterize its Zn(II)- and Cu(I)-binding behaviour, were heterologously produced in Escherichia coli cultures supplemented with Cd(II), and the corresponding complexes were purified up to homogeneity. The Cd(II)-binding ability of these recombinant peptides was determined through the chemical, spectroscopic and spectrometric characterization of the recovered clusters. Recombinant synthesis of the four QsMT peptides in cadmium-rich media rendered complexes with a higher metal content than those obtained from zinc-supplemented cultures and, consequently, the recovered Cd(II) species are nonisostructural to those of Zn(II). Also of interest is the fact that three out of the four peptides yielded recombinant preparations that included S(2-)-containing Cd(II) complexes as major species. Subsequently, the in vitro Zn(II)/Cd(II) replacement reactions were studied, as well as the in vitro acid denaturation and S(2-) renaturation reactions. Finally, the capacity of the four peptides for preventing cadmium deleterious effects in yeast cells was tested through complementation assays. Consideration of all the results enables us to suggest a hairpin folding model for this typical type 2 plant Cd(II)-MT complex, as well as a nonnegligible role of the spacer in the detoxification function of QsMT towards cadmium.</style></abstract><accession-num><style face="normal" font="default" size="100%">17503092</style></accession-num></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Grill, D</style></author><author><style face="normal" font="default" size="100%">Müller, M</style></author><author><style face="normal" font="default" size="100%">Tausz, M</style></author><author><style face="normal" font="default" size="100%">Strnad, B</style></author><author><style face="normal" font="default" size="100%">Wonisch, A</style></author><author><style face="normal" font="default" size="100%">Raschi, A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effects of sulphurous gases in two CO2 springs on total sulphur and thiols in acorns and oak seedlings</style></title><secondary-title><style face="normal" font="default" size="100%">Atmospheric Environment</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cytogenetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutathione</style></keyword><keyword><style  face="normal" font="default" size="100%">hydrogen sulphide</style></keyword><keyword><style  face="normal" font="default" size="100%">Stress</style></keyword><keyword><style  face="normal" font="default" size="100%">Sulphur dioxide</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year></dates><volume><style face="normal" font="default" size="100%">38</style></volume><pages><style face="normal" font="default" size="100%">3775-3780</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Quercus ilex and Quercus pubescens acorns were collected at two CO2 springs in Tuscany (Bossoleto and Viterbo, resp.). In addition to elevated CO2, these springs are a source of H2S and SO2 . Acorns from a comparable ﬁeld site distant from CO2 springs were used as controls. Acorns from CO2 springs contained signiﬁcantly higher sulphur concentrations than controls (0.67 vs. 0.47 mg g 1 dw in Q. ilex cotyledons and 1.01 vs. 0.80 in Q. pubescens) and, in Q. ilex, also more glutathione (1634 vs. 1393 nmol g 1 dw). When acorns were germinated and seedlings grown under ambient air conditions in the Botanical Garden in Graz for one year, leaves of Q. pubescens grown from CO2 spring acorns showed signiﬁcantly higher S-concentrations than leaves grown from control acorns (2.27 mg g 1 vs. 1.56 mg g 1 dw), and those of Q. ilex higher glutathione concentrations (929 vs. 462 nmol g 1 dw, CO2 spring vs. control acorns). One-year-old Q. ilex seedlings grown from CO2 spring acorns also showed elevated rates of chromosomal aberrations in root tips (a widely used test for environmental impacts), suggesting a permanent stress situation of the seedlings originating from the CO2 springs.</style></abstract></record></records></xml>