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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Detalles Bibliográficos
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

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