caa a22 4500 605507430 CHVBK 20210128100632.0 cr unu---uuuuu 210128e20150601xx s 000 0 eng 10.1007/s00775-015-1259-1 doi (NATIONALLICENCE)springer-10.1007/s00775-015-1259-1 EPR and NMR spectroscopies provide input on the coordination of Cu(I) and Ag(I) to a disordered methionine segment [Elektronische Daten] [Yulia Shenberger, Hugo Gottlieb, Sharon Ruthstein] Methionine motifs are methionine-rich metal-binding segments found in many human, yeast, and bacterial proteins involved in the transportation of copper ion to other cellular pathways, and in protecting copper from oxidation. Methionine motifs are found to bind Ag(I) and Cu(I) ions. Proteins or peptides that can bind different metal ions should have the ability to differentiate between them, to be able to shuttle them to various pathways in the cell. This study utilizes electron paramagnetic resonance spectroscopy together with circular dichroism and nuclear magnetic resonance to probe structural changes in the methionine segment upon coordinating Cu(I) and Ag(I) metal ions. The data collected here indicate that methionine segments experience structural changes while coordinating Cu(I) and Ag(I), however, the differences between the coordination of Cu(I) vs. Ag(I) to the methionine segment are mild. Since Cu(I) and Ag(I) metal ions are pretty similar in their nature and charge, the minor structural changes reported here are significant towards the understanding of the differences in the transport mechanism of these two metalions in prokaryotic and eukaryotic cells. SBIC, 2015 Methionine segments nationallicence Cu(I)/Ag(I) transport nationallicence DEER nationallicence Q-band nationallicence Site-directed spin labeling nationallicence CD : Circular dichroism nationallicence CW : Continuous wave nationallicence DEER : Double electron-electron resonance nationallicence EPR : Electron paramagnetic resonance nationallicence Met : Methionine nationallicence 5-MSL : 3-Maleimido-proxyl nationallicence MTSSL : (1-Oxyl-2,2,5,5-tetramethyl-2,5-pyrroline-3-methyl) methanethiosulfonate nationallicence NMR : Nuclear magnetic resonance nationallicence SDSL : Site-directed spin-labeling nationallicence Shenberger Yulia The Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, 5290002, Ramat-Gan, Israel aut Gottlieb Hugo The Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, 5290002, Ramat-Gan, Israel aut Ruthstein Sharon The Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, 5290002, Ramat-Gan, Israel aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/4(2015-06-01), 719-727 0949-8257 20:4<719 2015 20 775 https://doi.org/10.1007/s00775-015-1259-1 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-015-1259-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shenberger Yulia The Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, 5290002, Ramat-Gan, Israel aut NATIONALLICENCE 700 1- Gottlieb Hugo The Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, 5290002, Ramat-Gan, Israel aut NATIONALLICENCE 700 1- Ruthstein Sharon The Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, 5290002, Ramat-Gan, Israel aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/4(2015-06-01), 719-727 0949-8257 20:4<719 2015 20 775