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Abstract:

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.

Registro:

Documento: Artículo
Título:Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c
Autor:Alvarez-Paggi, D.; Castro, M.A.; Tórtora, V.; Castro, L.; Radi, R.; Murgida, D.H.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pab. 2, piso 1, C1428EHA-Buenos Aires, Argentina
INQUIMAE (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pab. 2, piso 1, C1428EHA-Buenos Aires, Argentina
Departamento de Bioquímica, Uruguay
Center for Free Radical and Biomedical Research, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay
Palabras clave: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
Año:2013
Volumen:135
Número:11
Página de inicio:4389
Página de fin:4397
DOI: http://dx.doi.org/10.1021/ja311786b
Título revista:Journal of the American Chemical Society
Título revista abreviado:J. Am. Chem. Soc.
ISSN:00027863
CODEN:JACSA
CAS:cytochrome c, 9007-43-6, 9064-84-0; heme, 14875-96-8; iron, 14093-02-8, 53858-86-9, 7439-89-6; Cytochromes c, 9007-43-6; Tyrosine, 55520-40-6
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v135_n11_p4389_AlvarezPaggi

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Citas:

---------- APA ----------
Alvarez-Paggi, D., Castro, M.A., Tórtora, V., Castro, L., Radi, R. & Murgida, D.H. (2013) . Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c. Journal of the American Chemical Society, 135(11), 4389-4397.
http://dx.doi.org/10.1021/ja311786b
---------- CHICAGO ----------
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" . Journal of the American Chemical Society 135, no. 11 (2013) : 4389-4397.
http://dx.doi.org/10.1021/ja311786b
---------- MLA ----------
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" . Journal of the American Chemical Society, vol. 135, no. 11, 2013, pp. 4389-4397.
http://dx.doi.org/10.1021/ja311786b
---------- VANCOUVER ----------
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. J. Am. Chem. Soc. 2013;135(11):4389-4397.
http://dx.doi.org/10.1021/ja311786b