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Hidricidad termodinámica de las [FeFe]-hidrogenasas

Eric S Wiedner¹

¹Center for Molecular Electrocatalysis, Pacific Northwest National Laboratory , P.O. Box 999, K2-57, Richland , Washington 99352 , United States.

Journal of the American Chemical Society

|April 24, 2019

Resumen

Los estados de hidruro terminal en las [FeFe]-hidrogenasas ahora se entienden utilizando la hidricidad. Este parámetro termodinámico guía la investigación futura y el diseño de nuevos catalizadores moleculares inspirados en las estructuras enzimáticas.

Área de la Ciencia:

La bioquímica
Química bioorgánica
Catálisis

Sus antecedentes:

Los estados de hidruro terminal en las [FeFe]-hidrogenasas eran previamente evasivos.
La identificación reciente de estos estados en enzimas nativas y mutantes requiere una investigación adicional.

Objetivo del estudio:

Para analizar los estados hidruro de las [FeFe]-hidrogenasas en función de la hidricidad.
Explorar cómo la hidricidad puede informar la investigación futura de la hidrogenasa y el diseño de catalizadores sintéticos.
Establecer relaciones cuantitativas entre las variantes enzimáticas y sus propiedades catalíticas.

Principales métodos:

Análisis termodinámico utilizando la hidricidad.
Desarrollo de relaciones de energía libre lineal.
Comparación con los complejos de hidruro de metales de transición.
Propuesta mecanicista para efectos de enlace de hidrógeno.

Principales resultados:

La hidricidad proporciona un marco para comprender los estados de hidruro de la [FeFe]-hidrogenasa.
Se desarrollaron correlaciones cuantitativas entre las variantes enzimáticas y su actividad catalítica.
Se destacó una fuerte comunicación electrónica entre el sitio activo de diiron y el andamio de proteínas.
Se propuso un mecanismo para el enlace de hidrógeno que influye en la hidricidad.

Conclusiones:

La hidricidad es un parámetro clave para el estudio de las hidrogenasas [FeFe] y el diseño de catalizadores moleculares.
Se pueden aclarar más las relaciones estructura-actividad en las [FeFe]-hidrogenasas.
La emulación de las características estructurales de las enzimas en complejos sintéticos es factible.

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