The alkaline transition of cytochrome c revisited: Effects of electrostatic interactions and tyrosine nitration on the reaction dynamics

Here we investigated the effect of electrostatic interactions and of protein tyrosine nitration of mammalian cytochrome c on the dynamics of the so-called alkaline transition, a pH- and redox-triggered conformational change that implies replacement of the axial ligand Met80 by a Lys residue. Using a...

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Detalles Bibliográficos
Autores principales: Oviedo-Rouco, S., Castro, M.A., Alvarez-Paggi, D., Spedalieri, C., Tortora, V., Tomasina, F., Radi, R., Murgida, D.H.
Formato: JOUR
Materias:
Alkaline transition
Cytochrome c
Protein electron transfer
Protein nitration
Protein spectroelectrochemistry
Time-resolved SERR
cytochrome c
ligand
tyrosine
alkalinity
Article
cellular distribution
chemical reaction kinetics
conformational transition
cyclic potentiometry
deprotonation
electrochemical analysis
model
molecular dynamics
nitration
oxidation reduction reaction
pH
pKa
priority journal
protein conformation
Raman spectrometry
reaction analysis
static electricity
surface property
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v665_n_p96_OviedoRouco
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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