H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin

The ferric form of truncated hemoglobin II from Thermobifida fusca (Tf-trHb) and its triple mutant WG8F-YB10F-YCD1F at neutral and alkaline pH, and in the presence of CN- have been characterized by resonance Raman spectroscopy, electron paramagnetic resonance spectroscopy, and molecular dynamics sim...

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Detalles Bibliográficos
Autores principales: Nicoletti, F.P., Droghetti, E., Howes, B.D., Bustamante, J.P., Bonamore, A., Sciamanna, N., Estrin, D.A., Feis, A., Boffi, A., Smulevich, G.
Formato: JOUR
Materias:
Cyanide ligand
Hydrogen-bond
Hydroxyl ligand
Resonance Raman
Truncated hemoglobin
cyanide
hydroxyl group
ligand
truncated hemoglobin
tyrosine
water
heme
hemoglobin
hydroxide
hydroxide ion
myoglobin
alkalinity
article
electron spin resonance
hydrogen bond
ligand binding
molecular dynamics
molecule
nonhuman
priority journal
Raman spectrometry
static electricity
Thermobifida fusca
2-(N-morpholino)ethanesulfonic acid
5c
6c
acidic surface variant of Tf-trHb containing two single site mutations Phe107Glu and Arg91Glu
Actinomycetales
ASV
enzyme active site
five-coordinate
genetics
high spin
HS
low spin
LS
Mb
MD
MES
metabolism
pH
protein binding
RR
six-coordinate
Tf
trHb
wild type
WT
electron paramagnetic resonance
EPR
Hb
resonance Raman
Catalytic Domain
Cyanides
Heme
Hemoglobins
Hydrogen Bonding
Hydrogen-Ion Concentration
Hydroxides
Molecular Dynamics Simulation
Protein Binding
Spectrum Analysis, Raman
Tyrosine
Water
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15709639_v1834_n9_p1901_Nicoletti
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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