Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release

Carbon monoxide releasing molecules (CORMs) have important bactericidal, anti-inflammatory, neuroprotective, and antiapoptotic effects and can be used as tools for CO physiology experiments, including studies on vasodilation. In this context, a new class of CO releasing molecules, based on pentachlo...

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Detalles Bibliográficos
Publicado:	2014
Materias:	carbon monoxide hen egg lysozyme iridium lysozyme organometallic compound chemistry metabolism molecular dynamics synthesis Carbon Monoxide Iridium Molecular Dynamics Simulation Muramidase Organometallic Compounds
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v53_n19_p10456_Petruk http://hdl.handle.net/20.500.12110/paper_00201669_v53_n19_p10456_Petruk
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00201669_v53_n19_p10456_Petruk
record_format	dspace
spelling	paper:paper_00201669_v53_n19_p10456_Petruk2023-06-08T14:40:43Z Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release carbon monoxide hen egg lysozyme iridium lysozyme organometallic compound chemistry metabolism molecular dynamics synthesis Carbon Monoxide Iridium Molecular Dynamics Simulation Muramidase Organometallic Compounds Carbon monoxide releasing molecules (CORMs) have important bactericidal, anti-inflammatory, neuroprotective, and antiapoptotic effects and can be used as tools for CO physiology experiments, including studies on vasodilation. In this context, a new class of CO releasing molecules, based on pentachlorocarbonyliridate(III) derivative have been recently reported. Although there is a growing interest in the characterization of protein-CORMs interactions, only limited structural information on CORM binding to protein and CO release has been available to date. Here, we report six different crystal structures describing events ranging from CORM entrance into the protein crystal up to the CO release and a biophysical characterization by isothermal titration calorimetry, Raman microspectroscopy, and molecular dynamics simulations of the complex between a pentachlorocarbonyliridate(III) derivative and hen egg white lysozyme, a model protein. Altogether, the data indicate the formation of a complex in which the ligand can bind to different sites of the protein surface and provide clues on the mechanism of adduct formation and CO release. © 2014 American Chemical Society. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v53_n19_p10456_Petruk http://hdl.handle.net/20.500.12110/paper_00201669_v53_n19_p10456_Petruk
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	carbon monoxide hen egg lysozyme iridium lysozyme organometallic compound chemistry metabolism molecular dynamics synthesis Carbon Monoxide Iridium Molecular Dynamics Simulation Muramidase Organometallic Compounds
spellingShingle	carbon monoxide hen egg lysozyme iridium lysozyme organometallic compound chemistry metabolism molecular dynamics synthesis Carbon Monoxide Iridium Molecular Dynamics Simulation Muramidase Organometallic Compounds Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release
topic_facet	carbon monoxide hen egg lysozyme iridium lysozyme organometallic compound chemistry metabolism molecular dynamics synthesis Carbon Monoxide Iridium Molecular Dynamics Simulation Muramidase Organometallic Compounds
description	Carbon monoxide releasing molecules (CORMs) have important bactericidal, anti-inflammatory, neuroprotective, and antiapoptotic effects and can be used as tools for CO physiology experiments, including studies on vasodilation. In this context, a new class of CO releasing molecules, based on pentachlorocarbonyliridate(III) derivative have been recently reported. Although there is a growing interest in the characterization of protein-CORMs interactions, only limited structural information on CORM binding to protein and CO release has been available to date. Here, we report six different crystal structures describing events ranging from CORM entrance into the protein crystal up to the CO release and a biophysical characterization by isothermal titration calorimetry, Raman microspectroscopy, and molecular dynamics simulations of the complex between a pentachlorocarbonyliridate(III) derivative and hen egg white lysozyme, a model protein. Altogether, the data indicate the formation of a complex in which the ligand can bind to different sites of the protein surface and provide clues on the mechanism of adduct formation and CO release. © 2014 American Chemical Society.
title	Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release
title_short	Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release
title_full	Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release
title_fullStr	Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release
title_full_unstemmed	Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release
title_sort	interaction between proteins and ir based co releasing molecules: mechanism of adduct formation and co release
publishDate	2014
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v53_n19_p10456_Petruk http://hdl.handle.net/20.500.12110/paper_00201669_v53_n19_p10456_Petruk
_version_	1768544943644606464

Interaction between proteins and Ir based CO releasing molecules: Mechanism of adduct formation and CO release

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