The N-terminal pre-A region of Mycobacterium tuberculosis 2/2HbN promotes NO-dioxygenase activity

A unique defense mechanisms by which Mycobacterium tuberculosis protects itself from nitrosative stress is based on the O2-dependent NO-dioxygenase (NOD) activity of truncated hemoglobin 2/2HbN (Mt2/2HbN). The NOD activity largely depends on the efficiency of ligand migration to the heme cavity thro...

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Detalles Bibliográficos
Autores principales: Pesce, A., Bustamante, J.P., Bidon-Chanal, A., Boechi, L., Estrin, D.A., Luque, F.J., Sebilo, A., Guertin, M., Bolognesi, M., Ascenzi, P., Nardini, M.
Formato: JOUR
Materias:
2/2 hemoglobins
globin dynamics
heme/ligand tunneling
NO dioxygenase
truncated hemoglobins
bacterial protein
dioxygenase
heme
nitric oxide
peroxynitrous acid
truncated hemoglobin
chemistry
genetics
kinetics
metabolism
molecular dynamics
mutation
Mycobacterium tuberculosis
protein conformation
protein multimerization
X ray crystallography
Bacterial Proteins
Crystallography, X-Ray
Dioxygenases
Heme
Kinetics
Molecular Dynamics Simulation
Mutation
Nitric Oxide
Peroxynitrous Acid
Protein Conformation
Protein Multimerization
Truncated Hemoglobins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_1742464X_v283_n2_p305_Pesce
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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