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Enlace de dinitrógeno a un sitio de hierro-azufre-carbono

Ilija Čorić¹, Brandon Q Mercado¹, Eckhard Bill²

¹Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, USA.

|September 30, 2015

Resumen

Las enzimas nitrogenasas convierten el nitrógeno atmosférico (N2) en amoníaco. Los investigadores crearon un complejo de hierro sintético que imita este proceso, revelando cómo el N2 se une a la enzima

Área de la Ciencia:

La bioquímica
Química inorgánica
Química bioorgánica

Sus antecedentes:

Las nitrogenasas catalizan la conversión del nitrógeno atmosférico (N2) en amoníaco, esencial para la vida.
El cofactor hierro-molibdeno (FeMoco) es el sitio activo, con coordinación hierro- azufre-carbono.
El mecanismo preciso de unión de N2 en FeMoco sigue siendo elusivo.

Objetivo del estudio:

Para aclarar el mecanismo de unión de N2 en el sitio activo de FeMoco.
Desarrollar un modelo sintético para la coordinación de N2 en las nitrogenasas.
Investigar el papel de la escisión del enlace Fe-S en la activación de N2.

Principales métodos:

Síntesis de un nuevo complejo de hierro con una esfera de coordinación rica en azufre.
Reducción electroquímica del complejo sintético.
Caracterización estructural y espectroscópica de las especies ligadas al N2.

Principales resultados:

El complejo sintético, después de la reducción, se somete a la escisión de enlaces Fe-S.
Esta escisión facilita la unión del N2 al centro del hierro.
El complejo resultante es la primera especie sintética Fe-N2 con coordinación Fe-S-C, modelado FeMoco.
Los datos estructurales y espectroscópicos detallados revelan un enlace N2 debilitado.

Conclusiones:

La ruptura del enlace Fe-S es un mecanismo viable para la unión de N2 en FeMoco.
El modelo sintético proporciona información crucial sobre el ciclo catalítico de la nitrogenasa.
Este estudio hace avanzar nuestra comprensión de la fijación biológica del nitrógeno.

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