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
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.. - In: DALTON TRANSACTIONS. - ISSN 1477-9226. - 45:30(2016), pp. 12206-12214. [10.1039/c6dt01685e]
Mapping the protein-binding sites for iridium(III)-based CO-releasing molecules
CATERINO, MARCO;VERGARA, ALESSANDRO;FERRARO, GIARITA;MARASCO, DANIELA;MERLINO, ANTONELLO
2016
Abstract
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 propertiesI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
