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spelling 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
repository_str R-134
collection 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
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