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No inocencia del ligando del tiolato/disulfuro en complejos dinucleares de cobre: isomerización redox dependiente del

Andrew M Thomas¹, Bo-Lin Lin, Erik C Wasinger

¹Department of Chemistry, Stanford University , Stanford, California 94305, United States.

Journal of the American Chemical Society

|November 28, 2013

Resumen

Los complejos sintéticos de cobre imitan los procesos de redox de proteínas, mostrando interconversiones dependientes del disolvente entre las formas de tiolato y disulfuro. La adición de protones impulsa la transferencia de electrones, revelando los mecanismos para la gestión de iones de cobre en los sistemas biológicos.

Área de la Ciencia:

Química bioorgánica Química bioorgánica.
Coordinación Química de la Coordinación
La bioquímica es la bioquímica.

Sus antecedentes:

Las interconversiones de tiolato de cobre/disulfuro son cruciales en proteínas como el Sco1 humano y el SOD1.1.
La comprensión de estos procesos redox requiere análogos sintéticos bien definidos.

Objetivo del estudio:

Para sintetizar y caracterizar complejos de cobre dimérico que imitan las interconversiones de proteínas.
Para investigar la isomerización redox dependiente del disolvente y la transferencia de electrones acoplados a protones.

Principales métodos:

Difracción de rayos X por difracción de rayos X.
La espectroscopia de absorción de rayos X (XAS, por sus siglas en inglés)
La Resonancia Magnética Nuclear (RMN) es una técnica de resonancia nuclear.
Espectroscopia visible en rayos UV.

Principales resultados:

Se observó un equilibrio dependiente del disolvente entre las formas diméricas μ-tiolato Cu{II}Cu{II} y μ-disulfido Cu{I}Cu{I}.
La adición de protones (2 equiv) indujo la formación completa del complejo μ-disulfuro Cu(I) Cu(I) a través de la transferencia de electrones acoplados a protones.
La eliminación de protones revirtió la reacción, lo que demuestra la protonación / desprotonación reversible.

Conclusiones:

El estudio presenta un nuevo precedente químico para el manejo de iones de cobre en sistemas biológicos.
Los mecanismos observados de protonación reductora / desprotonación oxidativa ofrecen información sobre la función de las metaloproteínas.

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