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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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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spelling	todo:paper_00027863_v135_n11_p4389_AlvarezPaggi2023-10-03T13:54:22Z Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c Alvarez-Paggi, D. Castro, M.A. Tórtora, V. Castro, L. Radi, R. Murgida, D.H. 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 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-protein and protein-lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first-(M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer. © 2013 American Chemical Society. Fil:Alvarez-Paggi, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Castro, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00027863_v135_n11_p4389_AlvarezPaggi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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
spellingShingle	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 Alvarez-Paggi, D. Castro, M.A. Tórtora, V. Castro, L. Radi, R. Murgida, D.H. Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
topic_facet	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
description	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-protein and protein-lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first-(M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer. © 2013 American Chemical Society.
format	JOUR
author	Alvarez-Paggi, D. Castro, M.A. Tórtora, V. Castro, L. Radi, R. Murgida, D.H.
author_facet	Alvarez-Paggi, D. Castro, M.A. Tórtora, V. Castro, L. Radi, R. Murgida, D.H.
author_sort	Alvarez-Paggi, D.
title	Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
title_short	Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
title_full	Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
title_fullStr	Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
title_full_unstemmed	Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
title_sort	electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
url	http://hdl.handle.net/20.500.12110/paper_00027863_v135_n11_p4389_AlvarezPaggi
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_version_	1807322625199833088

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

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