Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases

The binding of diatomic ligands, such as O2, NO, and CO, to heme proteins is a process intimately related with their function. In this work, we analyzed by means of a combination of classical Molecular Dynamics (MD) and Hybrid Quantum-Classical (QM/MM) techniques the existence of multiple conformati...

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Autores principales:	Martí, M.A., Capece, L., Bikiel, D.E., Falcone, B., Estrin, D.A.
Formato:	JOUR
Materias:	Heme protein Hydrogen bond Ligand binding Molecular dynamics QM/MM Structure carbon monoxide hemoglobin leghemoglobin nitric oxide oxygen article computer simulation enthalpy hydrogen bond molecular dynamics mutation nonhuman oxygen affinity Paramecium caudatum priority journal protein conformation quantum chemistry soybean Animals Binding Sites Computer Simulation Hemoglobins Kinetics Leghemoglobin Models, Molecular Oxygen Plant Proteins Protein Conformation Protozoan Proteins Soybeans Glycine max
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_08873585_v68_n2_p480_Marti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_08873585_v68_n2_p480_Marti
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spelling	todo:paper_08873585_v68_n2_p480_Marti2023-10-03T15:40:50Z Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases Martí, M.A. Capece, L. Bikiel, D.E. Falcone, B. Estrin, D.A. Heme protein Hydrogen bond Ligand binding Molecular dynamics QM/MM Structure carbon monoxide hemoglobin leghemoglobin nitric oxide oxygen article computer simulation enthalpy hydrogen bond molecular dynamics mutation nonhuman oxygen affinity Paramecium caudatum priority journal protein conformation quantum chemistry soybean Animals Binding Sites Computer Simulation Hemoglobins Kinetics Leghemoglobin Models, Molecular Oxygen Paramecium caudatum Plant Proteins Protein Conformation Protozoan Proteins Soybeans Glycine max Paramecium caudatum The binding of diatomic ligands, such as O2, NO, and CO, to heme proteins is a process intimately related with their function. In this work, we analyzed by means of a combination of classical Molecular Dynamics (MD) and Hybrid Quantum-Classical (QM/MM) techniques the existence of multiple conformations in the distal site of heme proteins and their influence on oxygen affinity regulation. We considered two representative examples: soybean leghemoglobin (Lba) and Paramecium caudatum truncated hemoglobin (PcHb). The results presented in this work provide a molecular interpretation for the kinetic, structural, and mutational data that cannot be obtained by assuming a single distal conformation. © 2007 Wiley-Liss, Inc. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Capece, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Bikiel, D.E. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08873585_v68_n2_p480_Marti
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Heme protein Hydrogen bond Ligand binding Molecular dynamics QM/MM Structure carbon monoxide hemoglobin leghemoglobin nitric oxide oxygen article computer simulation enthalpy hydrogen bond molecular dynamics mutation nonhuman oxygen affinity Paramecium caudatum priority journal protein conformation quantum chemistry soybean Animals Binding Sites Computer Simulation Hemoglobins Kinetics Leghemoglobin Models, Molecular Oxygen Paramecium caudatum Plant Proteins Protein Conformation Protozoan Proteins Soybeans Glycine max Paramecium caudatum
spellingShingle	Heme protein Hydrogen bond Ligand binding Molecular dynamics QM/MM Structure carbon monoxide hemoglobin leghemoglobin nitric oxide oxygen article computer simulation enthalpy hydrogen bond molecular dynamics mutation nonhuman oxygen affinity Paramecium caudatum priority journal protein conformation quantum chemistry soybean Animals Binding Sites Computer Simulation Hemoglobins Kinetics Leghemoglobin Models, Molecular Oxygen Paramecium caudatum Plant Proteins Protein Conformation Protozoan Proteins Soybeans Glycine max Paramecium caudatum Martí, M.A. Capece, L. Bikiel, D.E. Falcone, B. Estrin, D.A. Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
topic_facet	Heme protein Hydrogen bond Ligand binding Molecular dynamics QM/MM Structure carbon monoxide hemoglobin leghemoglobin nitric oxide oxygen article computer simulation enthalpy hydrogen bond molecular dynamics mutation nonhuman oxygen affinity Paramecium caudatum priority journal protein conformation quantum chemistry soybean Animals Binding Sites Computer Simulation Hemoglobins Kinetics Leghemoglobin Models, Molecular Oxygen Paramecium caudatum Plant Proteins Protein Conformation Protozoan Proteins Soybeans Glycine max Paramecium caudatum
description	The binding of diatomic ligands, such as O2, NO, and CO, to heme proteins is a process intimately related with their function. In this work, we analyzed by means of a combination of classical Molecular Dynamics (MD) and Hybrid Quantum-Classical (QM/MM) techniques the existence of multiple conformations in the distal site of heme proteins and their influence on oxygen affinity regulation. We considered two representative examples: soybean leghemoglobin (Lba) and Paramecium caudatum truncated hemoglobin (PcHb). The results presented in this work provide a molecular interpretation for the kinetic, structural, and mutational data that cannot be obtained by assuming a single distal conformation. © 2007 Wiley-Liss, Inc.
format	JOUR
author	Martí, M.A. Capece, L. Bikiel, D.E. Falcone, B. Estrin, D.A.
author_facet	Martí, M.A. Capece, L. Bikiel, D.E. Falcone, B. Estrin, D.A.
author_sort	Martí, M.A.
title	Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
title_short	Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
title_full	Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
title_fullStr	Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
title_full_unstemmed	Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
title_sort	oxygen affinity controlled by dynamical distal conformations: the soybean leghemoglobin and the paramecium caudatum hemoglobin cases
url	http://hdl.handle.net/20.500.12110/paper_08873585_v68_n2_p480_Marti
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Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases

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