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Reactividad hemo/Cu/O2: cambio en la geometría de unión peroxo de la unidad FeIII-(O2 2-) -CuII efectuado por la

Eunsuk Kim¹, Jason Shearer, Shen Lu

¹Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.

Journal of the American Chemical Society

|October 8, 2004

Resumen

Los investigadores crearon un nuevo complejo hemo-peroxo-cobre con una ligadura peroxo lateral única. Este descubrimiento avanza en la comprensión de la química del oxígeno en los sitios activos de la hemo-cobre oxidasa.

Área de la Ciencia:

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

Sus antecedentes:

Los centros hemo-cobre son cruciales en la reducción biológica del oxígeno.
Comprender sus mecanismos de activación de O2 es clave para la función de las enzimas.

Objetivo del estudio:

Para sintetizar y caracterizar un nuevo complejo hemo-peroxo-cobre.
Para aclarar las propiedades estructurales y electrónicas de la peroxoligación.
Para obtener información sobre la química del sitio activo de la hemo-cobre oxidasa.

Principales métodos:

Síntesis de ligandos heterobinucleantes.
Oxigenación de un complejo Fe (II) Cu (I) a bajas temperaturas.
Análisis cinético y espectroscópico de flujo detenido.
Resonancia Raman y espectroscopia de absorción de rayos X.

Principales resultados:

Formación de un intermediario superoxo transitorio seguido de una reacción intramolecular.
Caracterización de un nuevo complejo mu-eta2:eta2 peroxo-cobre.
La espectroscopia Raman de resonancia confirmó una baja frecuencia de estiramiento O-O indicativa de la unión lateral.
La espectroscopia de absorción de rayos X apoyó un centro de cobre de cinco coordenadas y un grupo peroxo unido simétricamente.

Conclusiones:

Se generó con éxito un nuevo tipo estructural de complejo hemo-peroxo-cobre con ligadura peroxo mu-eta2:eta2.
La unión lateral del peróxido al cobre está confirmada por datos espectroscópicos y EXAFS.
Este estudio proporciona información fundamental sobre la química del O2 relevante para los sitios activos de la hemo-cobre oxidasa.

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