Heme protein oxygen affinity regulation exerted by proximal effects

Heme proteins are found in all living organisms and are capable of performing a wide variety of tasks, requiring in many cases the binding of diatomic ligands, namely, O2, CO, and/or NO. Therefore, subtle regulation of these diatomic ligands' affinity is one of the key issues for determining a...

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Autores principales:	Capece, Luciana, Martí, Marcelo Adrián, Crespo, Alejandro, Doctorovich, Fabio Ariel, Estrin, Dario Ariel
Publicado:	2006
Materias:	Hemoglobin Hydrogen bonds Oxygen Probability density function Quantum theory Density functional theory Heme proteins Ligands Oxygen affinity Proteins carbon monoxide hemoprotein histidine derivative iron derivative leghemoglobin myoglobin nitric oxide oxygen porphyrin article binding affinity calculation computer simulation density functional theory hydrogen bond ligand binding oxygen affinity protein binding protein function Binding Sites Computer Simulation Ferrous Compounds Histidine Kinetics Leghemoglobin Models, Molecular Myoglobin Quantum Theory Thermodynamics
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v128_n38_p12455_Capece http://hdl.handle.net/20.500.12110/paper_00027863_v128_n38_p12455_Capece
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00027863_v128_n38_p12455_Capece
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spelling	paper:paper_00027863_v128_n38_p12455_Capece2023-06-08T14:22:41Z Heme protein oxygen affinity regulation exerted by proximal effects Capece, Luciana Martí, Marcelo Adrián Crespo, Alejandro Doctorovich, Fabio Ariel Estrin, Dario Ariel Hemoglobin Hydrogen bonds Oxygen Probability density function Quantum theory Density functional theory Heme proteins Ligands Oxygen affinity Proteins carbon monoxide hemoprotein histidine derivative iron derivative leghemoglobin myoglobin nitric oxide oxygen porphyrin article binding affinity calculation computer simulation density functional theory hydrogen bond ligand binding oxygen affinity protein binding protein function Binding Sites Computer Simulation Ferrous Compounds Histidine Kinetics Leghemoglobin Models, Molecular Myoglobin Oxygen Quantum Theory Thermodynamics Heme proteins are found in all living organisms and are capable of performing a wide variety of tasks, requiring in many cases the binding of diatomic ligands, namely, O2, CO, and/or NO. Therefore, subtle regulation of these diatomic ligands' affinity is one of the key issues for determining a heme protein's function. This regulation is achieved through direct H-bond interactions between the bound ligand and the protein, and by subtle tuning of the intrinsic heme group reactivity. In this work, we present an investigation of the proximal regulation of oxygen affinity in Fe(II) histidine coordinated heme proteins by means of computer simulation. Density functional theory calculations on heme model systems are used to analyze three proximal effects: charge donation, rotational position, and distance to the heme porphyrin plane of the proximal histidine. In addition, hybrid quantum-classical (QM-MM) calculations were performed in two representative proteins: myoglobin and leghemoglobin. Our results show that all three effects are capable of tuning the Fe-O2 bond strength in a cooperative way, consistently with the experimental data on oxygen affinity. The proximal effects described herein could operate in a large variety of O2-binding heme proteins-in combination with distal effects-and are essential to understand the factors determining a heme protein's O2 affinity. © 2006 American Chemical Society. Fil:Capece, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Marti, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Crespo, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Doctorovich, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2006 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v128_n38_p12455_Capece http://hdl.handle.net/20.500.12110/paper_00027863_v128_n38_p12455_Capece
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Hemoglobin Hydrogen bonds Oxygen Probability density function Quantum theory Density functional theory Heme proteins Ligands Oxygen affinity Proteins carbon monoxide hemoprotein histidine derivative iron derivative leghemoglobin myoglobin nitric oxide oxygen porphyrin article binding affinity calculation computer simulation density functional theory hydrogen bond ligand binding oxygen affinity protein binding protein function Binding Sites Computer Simulation Ferrous Compounds Histidine Kinetics Leghemoglobin Models, Molecular Myoglobin Oxygen Quantum Theory Thermodynamics
spellingShingle	Hemoglobin Hydrogen bonds Oxygen Probability density function Quantum theory Density functional theory Heme proteins Ligands Oxygen affinity Proteins carbon monoxide hemoprotein histidine derivative iron derivative leghemoglobin myoglobin nitric oxide oxygen porphyrin article binding affinity calculation computer simulation density functional theory hydrogen bond ligand binding oxygen affinity protein binding protein function Binding Sites Computer Simulation Ferrous Compounds Histidine Kinetics Leghemoglobin Models, Molecular Myoglobin Oxygen Quantum Theory Thermodynamics Capece, Luciana Martí, Marcelo Adrián Crespo, Alejandro Doctorovich, Fabio Ariel Estrin, Dario Ariel Heme protein oxygen affinity regulation exerted by proximal effects
topic_facet	Hemoglobin Hydrogen bonds Oxygen Probability density function Quantum theory Density functional theory Heme proteins Ligands Oxygen affinity Proteins carbon monoxide hemoprotein histidine derivative iron derivative leghemoglobin myoglobin nitric oxide oxygen porphyrin article binding affinity calculation computer simulation density functional theory hydrogen bond ligand binding oxygen affinity protein binding protein function Binding Sites Computer Simulation Ferrous Compounds Histidine Kinetics Leghemoglobin Models, Molecular Myoglobin Oxygen Quantum Theory Thermodynamics
description	Heme proteins are found in all living organisms and are capable of performing a wide variety of tasks, requiring in many cases the binding of diatomic ligands, namely, O2, CO, and/or NO. Therefore, subtle regulation of these diatomic ligands' affinity is one of the key issues for determining a heme protein's function. This regulation is achieved through direct H-bond interactions between the bound ligand and the protein, and by subtle tuning of the intrinsic heme group reactivity. In this work, we present an investigation of the proximal regulation of oxygen affinity in Fe(II) histidine coordinated heme proteins by means of computer simulation. Density functional theory calculations on heme model systems are used to analyze three proximal effects: charge donation, rotational position, and distance to the heme porphyrin plane of the proximal histidine. In addition, hybrid quantum-classical (QM-MM) calculations were performed in two representative proteins: myoglobin and leghemoglobin. Our results show that all three effects are capable of tuning the Fe-O2 bond strength in a cooperative way, consistently with the experimental data on oxygen affinity. The proximal effects described herein could operate in a large variety of O2-binding heme proteins-in combination with distal effects-and are essential to understand the factors determining a heme protein's O2 affinity. © 2006 American Chemical Society.
author	Capece, Luciana Martí, Marcelo Adrián Crespo, Alejandro Doctorovich, Fabio Ariel Estrin, Dario Ariel
author_facet	Capece, Luciana Martí, Marcelo Adrián Crespo, Alejandro Doctorovich, Fabio Ariel Estrin, Dario Ariel
author_sort	Capece, Luciana
title	Heme protein oxygen affinity regulation exerted by proximal effects
title_short	Heme protein oxygen affinity regulation exerted by proximal effects
title_full	Heme protein oxygen affinity regulation exerted by proximal effects
title_fullStr	Heme protein oxygen affinity regulation exerted by proximal effects
title_full_unstemmed	Heme protein oxygen affinity regulation exerted by proximal effects
title_sort	heme protein oxygen affinity regulation exerted by proximal effects
publishDate	2006
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v128_n38_p12455_Capece http://hdl.handle.net/20.500.12110/paper_00027863_v128_n38_p12455_Capece
work_keys_str_mv	AT capeceluciana hemeproteinoxygenaffinityregulationexertedbyproximaleffects AT martimarceloadrian hemeproteinoxygenaffinityregulationexertedbyproximaleffects AT crespoalejandro hemeproteinoxygenaffinityregulationexertedbyproximaleffects AT doctorovichfabioariel hemeproteinoxygenaffinityregulationexertedbyproximaleffects AT estrindarioariel hemeproteinoxygenaffinityregulationexertedbyproximaleffects
_version_	1768544800207798272

Heme protein oxygen affinity regulation exerted by proximal effects

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