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Interacción del ligando de metionina en una proteína de cobre azul caracterizada por espectroscopia infrarroja

Amanda L Le Sueur¹, Richard N Schaugaard¹, Mu-Hyun Baik¹

¹Department of Chemistry, Indiana University , 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.

Journal of the American Chemical Society

|May 11, 2016

Resumen

La espectroscopia infrarroja con sondas C-D revela cómo el ligando de metionina en las proteínas de cobre azul como la plastocyanin cambia cuando el centro de cobre se oxida o se reduce. Este método también muestra cómo la unión a otras proteínas afecta esta interacción.

Área de la Ciencia:

La bioquímica
Espectroscopia
Estructura de las proteínas

Sus antecedentes:

La estructura de las proteínas ajusta la reactividad del sitio metálico, crucial para las funciones biológicas.
En las proteínas de cobre azul, un enlace alargado a un ligando de metionina modula las propiedades redox del cobre.
Comprender los estados redox de las metaloproteínas es un desafío debido a las limitaciones experimentales.

Objetivo del estudio:

Para caracterizar los cambios localizados en el ligando de cobre Met97 en plastocyanin a través de varios estados.
Para investigar el impacto de la unión redox en el sitio del cobre.
Demostrar la utilidad de la espectroscopia de infrarrojos con sondas C-D para estudios de metaloproteínas.

Principales métodos:

Etiquetado selectivo del sitio con sondas vibratorias de carbono y deuterio (C-D).
Espectroscopia infrarroja (IR) para analizar los cambios vibratorios.
Cálculos de la teoría funcional de la densidad (DFT) para la validación teórica.

Principales resultados:

Las absorciones IR de (d3-metil) Met97 son relatores sensibles de las interacciones entre metales y ligandos.
Se observaron cambios espectrales localizados en estados oxidados, reducidos, sustituidos y desplegados.
La unión al citocromo f sugiere una mayor interacción Cu-S ((Met97) en el complejo.

Conclusiones:

La espectroscopia IR con sondas C-D proporciona información a nivel molecular sobre los estados redox de las metaloproteínas.
La interacción del ligando de metionina axial está modulada por el entorno proteico y la unión del socio redox.
Esta técnica ofrece información espacial localizada para el estudio de la dinámica de las metaloproteínas.

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