Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules
A combination of mass spectrometry, Raman microspectroscopy, circular dichroism and X-ray crystallography has been used to obtain detailed information on the reaction of an iridium-based CO-releasing molecule (Ir-CORM), Cs2IrCl5CO, with a model protein, bovine pancreatic ribonuclease. The results sh...
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Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_14779226_v45_n30_p12206_Caterino |
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todo:paper_14779226_v45_n30_p12206_Caterino2023-10-03T16:19:19Z Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules Caterino, M. Petruk, A.A. Vergara, A. Ferraro, G. Marasco, D. Doctorovich, F. Estrin, D.A. Merlino, A. Amino acids Binding sites Bins Biochemistry Crystallography Dichroism Iridium Mass spectrometry Molecules Proteins Biological properties Bovine pancreatic ribonuclease Model proteins N-terminals Protein targets Protein-binding sites Raman microspectroscopy Side-chains X ray crystallography carbon monoxide iridium protein protein binding binding site chemical structure chemistry circular dichroism mass spectrometry Raman spectrometry X ray crystallography Binding Sites Carbon Monoxide Circular Dichroism Crystallography, X-Ray Iridium Mass Spectrometry Molecular Structure Protein Binding Proteins Spectrum Analysis, Raman A combination of mass spectrometry, Raman microspectroscopy, circular dichroism and X-ray crystallography has been used to obtain detailed information on the reaction of an iridium-based CO-releasing molecule (Ir-CORM), Cs2IrCl5CO, with a model protein, bovine pancreatic ribonuclease. The results show that Ir-compound fragments bind to the N-terminal amine and close to histidine and methionine side chains, and the CO ligand is retained for a long time. The data provide helpful information for identifying protein targets for Ir-CORMs and for studying the mechanism that allows them to exhibit their interesting biological properties. © The Royal Society of Chemistry 2016. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14779226_v45_n30_p12206_Caterino |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Amino acids Binding sites Bins Biochemistry Crystallography Dichroism Iridium Mass spectrometry Molecules Proteins Biological properties Bovine pancreatic ribonuclease Model proteins N-terminals Protein targets Protein-binding sites Raman microspectroscopy Side-chains X ray crystallography carbon monoxide iridium protein protein binding binding site chemical structure chemistry circular dichroism mass spectrometry Raman spectrometry X ray crystallography Binding Sites Carbon Monoxide Circular Dichroism Crystallography, X-Ray Iridium Mass Spectrometry Molecular Structure Protein Binding Proteins Spectrum Analysis, Raman |
spellingShingle |
Amino acids Binding sites Bins Biochemistry Crystallography Dichroism Iridium Mass spectrometry Molecules Proteins Biological properties Bovine pancreatic ribonuclease Model proteins N-terminals Protein targets Protein-binding sites Raman microspectroscopy Side-chains X ray crystallography carbon monoxide iridium protein protein binding binding site chemical structure chemistry circular dichroism mass spectrometry Raman spectrometry X ray crystallography Binding Sites Carbon Monoxide Circular Dichroism Crystallography, X-Ray Iridium Mass Spectrometry Molecular Structure Protein Binding Proteins Spectrum Analysis, Raman Caterino, M. Petruk, A.A. Vergara, A. Ferraro, G. Marasco, D. Doctorovich, F. Estrin, D.A. Merlino, A. Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules |
topic_facet |
Amino acids Binding sites Bins Biochemistry Crystallography Dichroism Iridium Mass spectrometry Molecules Proteins Biological properties Bovine pancreatic ribonuclease Model proteins N-terminals Protein targets Protein-binding sites Raman microspectroscopy Side-chains X ray crystallography carbon monoxide iridium protein protein binding binding site chemical structure chemistry circular dichroism mass spectrometry Raman spectrometry X ray crystallography Binding Sites Carbon Monoxide Circular Dichroism Crystallography, X-Ray Iridium Mass Spectrometry Molecular Structure Protein Binding Proteins Spectrum Analysis, Raman |
description |
A combination of mass spectrometry, Raman microspectroscopy, circular dichroism and X-ray crystallography has been used to obtain detailed information on the reaction of an iridium-based CO-releasing molecule (Ir-CORM), Cs2IrCl5CO, with a model protein, bovine pancreatic ribonuclease. The results show that Ir-compound fragments bind to the N-terminal amine and close to histidine and methionine side chains, and the CO ligand is retained for a long time. The data provide helpful information for identifying protein targets for Ir-CORMs and for studying the mechanism that allows them to exhibit their interesting biological properties. © The Royal Society of Chemistry 2016. |
format |
JOUR |
author |
Caterino, M. Petruk, A.A. Vergara, A. Ferraro, G. Marasco, D. Doctorovich, F. Estrin, D.A. Merlino, A. |
author_facet |
Caterino, M. Petruk, A.A. Vergara, A. Ferraro, G. Marasco, D. Doctorovich, F. Estrin, D.A. Merlino, A. |
author_sort |
Caterino, M. |
title |
Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules |
title_short |
Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules |
title_full |
Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules |
title_fullStr |
Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules |
title_full_unstemmed |
Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules |
title_sort |
mapping the protein-binding sites for iridium(iii)-based co-releasing molecules |
url |
http://hdl.handle.net/20.500.12110/paper_14779226_v45_n30_p12206_Caterino |
work_keys_str_mv |
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_version_ |
1807321622485401600 |