Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c

We have employed a combination of protein film voltammetry, time-resolved vibrational spectroelectrochemistry and molecular dynamics simulations to evaluate the electron-transfer reorganization free energy (λ) of cytochrome c (Cyt) in electrostatic complexes that mimic some basic features of protein...

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Detalles Bibliográficos
Autores principales: Alvarez-Paggi, D., Castro, M.A., Tórtora, V., Castro, L., Radi, R., Murgida, D.H.
Formato: JOUR
Materias:
Conformational switches
Electrostatic complexes
Electrostatically driven
Molecular dynamics simulations
Protein film voltammetry
Protein-lipid interactions
Reorganization energies
Second-sphere ligands
Electrostatics
Ligands
Molecular dynamics
Spectroelectrochemistry
Proteins
cytochrome c
heme
iron
ligand
article
conformational transition
crystal structure
cyclic potentiometry
dipole
electrochemistry
electron transport
energy
hydrogen bond
molecular dynamics
oxidation reduction state
potentiometry
protein conformation
protein film voltametry
protein folding
protein immobilization
protein lipid interaction
protein protein interaction
protein structure
signal transduction
static electricity
temperature dependence
wild type
Animals
Cytochromes c
Electrochemical Techniques
Electron Transport
Horses
Hydrogen Bonding
Molecular Dynamics Simulation
Point Mutation
Spectrum Analysis, Raman
Static Electricity
Tyrosine
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00027863_v135_n11_p4389_AlvarezPaggi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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