Hydrophobic effect drives oxygen uptake in myoglobin via histidine E7

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Since the elucidation of the myoglobin (Mb) structure, a histidine residue on the E helix (His-E7) has been proposed to act as a gate with an open or closed conformation controlling access to the active site. Although it is believed that at low pH, the His-E7 gate is in its open conformation, the fu...

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Detalles Bibliográficos
Autores principales: Boechi, L., Arrar, M., Martí, M.A., Olson, J.S., Roitberg, A.E., Estrin, D.A.
Formato: JOUR
Materias:
Active site
Conceptual frameworks
Energy profile
Histidine residues
Hydrophobic effect
Hydrophobic sites
Molecular dynamics simulations
Open conformation
Oxygen migration
Oxygen uptake
Protonation state
Rate enhancement
Side-chains
Significant differences
Amino acids
Hydrophobicity
Ligands
Molecular dynamics
Oxygen
Protonation
Conformations
alanine
histidine
histidine E7
myoglobin
oxygen
tryptophan
unclassified drug
article
chemical structure
energy transfer
hydrophobicity
molecular dynamics
oxygen consumption
oxygen transport
priority journal
protein conformation
proton transport
Animals
Histidine
Humans
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Myoglobin
Protein Binding
Protein Structure, Secondary
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219258_v288_n9_p6754_Boechi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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