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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

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Dinámica del temblor de proteínas ultrarrápidas en el citocromo c.

Chen Zang¹, Jeffrey A Stevens, Justin J Link

¹Department of Physics, Program of Biophysics, The Ohio State University, 191 West Woodruff Avenue, Columbus, Ohio, 43210, USA.

Journal of the American Chemical Society

|February 11, 2009

Resumen

El citocromo c es el citocromo c.

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Área de la Ciencia:

La bioquímica es la bioquímica.
Dinámica de las proteínas Dinámica de las proteínas.
La espectroscopia es una técnica de espectroscopia.

Sus antecedentes:

El citocromo c es una proteína crucial en la respiración celular.
Comprender sus estados redox y su dinámica es clave para la función celular.

Objetivo del estudio:

Investigar la distinta dinámica del hemo y los cambios de conformación de las proteínas en el citocromo c. férrico y ferroso.
Para dilucidar los procesos ultrarrápidos después de la excitación del femtosegundo.

Principales métodos:

Espectroscopia de femtosegundos con longitudes de onda de sondeo visibles hasta UV.
Mutagénesis dirigida al sitio del citocromo c.
Análisis de la coordinación del hemo y la dinámica de relajación de las proteínas.

Principales resultados:

El citocromo c de hierro exhibe una disociación ultra rápida del ligando hemo (coordinación de 6 a 5 veces) y posterior reunión (7 ps), induciendo sacudidas de proteínas y cambios conformacionales globales (recuperación en 13 y 42 ps).
El citocromo c férrico mantiene la coordinación del hemo de 6 veces, con una dinámica limitada a los procesos locales del sitio (conversión interna, enfriamiento vibratorio) y una recuperación completa del estado fundamental en 10 ps, sin mostrar relajación global.
La dinámica de las proteínas difiere significativamente entre los dos estados redox.

Conclusiones:

El estado redox del citocromo c dicta su dinámica ultrarrápida y sus vías de relajación conformacional.
La dinámica del estado férrico implica cambios significativos en la coordinación del hemo y perturbaciones de proteínas a gran escala, a diferencia del estado férrico.
Estos hallazgos proporcionan una visión crítica de los mecanismos funcionales del citocromo c.