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Bases estructurales para el control del efector y el reconocimiento del socio redox en el citocromo P450
Sarvind Tripathi1, Huiying Li, Thomas L Poulos
1Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697-3900, USA.
Science (New York, N.Y.)
|June 8, 2013
Resumen
La estructura del citocromo P450cam complejo con putidaredoxina revela cómo se regula la transferencia de electrones. Putidaredoxina cambia P450cam a un estado abierto, lo que facilita la transferencia de electrones acoplados a protones.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Estructural Biología estructural.
- Enzimología Enzimología.
Sus antecedentes:
- Los citocromos P450 son enzimas cruciales para las reacciones de la monooxigenasa.
- La transferencia de electrones de los socios redox es esencial para la actividad de P450.
- Los datos estructurales sobre los complejos asociados de P450-redox son limitados, lo que dificulta la comprensión del control de la interacción.
Objetivo del estudio:
- Para dilucidar la base estructural de las interacciones de los socios de P450-redox.
- Para entender el papel de la putidaredoxina (Pdx) en la regulación de la actividad de la P450cam.
Principales métodos:
- Se utilizó cristalografía de rayos X para determinar las estructuras de P450cam oxidado y reducido complejo con Pdx.
- Se obtuvieron estructuras de alta resolución a 2,2 y 2,09 angstroms.
Principales resultados:
- La estructura cristalina reveló que Pdx favorece una conformación abierta de P450cam, contrariamente a las expectativas.
- Este estado abierto facilita la formación de una red de enlaces de hidrógeno mediada por agua.
- Esta red es crítica para permitir la transferencia de electrones acoplados a protones.
Conclusiones:
- La putidiredoxina actúa como un efector, induciendo una conformación abierta en P450cam.
- El estado abierto inducido por Pdx es esencial para el mecanismo de transferencia de electrones acoplados a protones en P450cam.
- Estos hallazgos proporcionan información estructural crítica sobre la regulación del complejo de socios redóxicos P450-redox.
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