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La azurina como un andamio proteico para un sitio de hierro no hemo de baja coordinación con un bolsillo de unión de

Matthew P McLaughlin¹, Marius Retegan, Eckhard Bill

¹Department of Chemistry, University of Rochester, Rochester, New York 14618, United States.

Journal of the American Chemical Society

|November 22, 2012

Resumen

Se llama Pseudomonas aeruginosa azurinosa.

Área de la Ciencia:

La bioquímica es la bioquímica.
Química bioorgánica Química bioorgánica.
Biología Estructural Biología estructural.

Sus antecedentes:

Pseudomonas aeruginosa azurin es una proteína que contiene cobre involucrada en la transferencia de electrones.
Comprender la química de coordinación de los iones metálicos en las proteínas es crucial para dilucidar su función.
La unión del hierro (II) a la azurina proporciona información sobre las propiedades del sitio activo de la metaloproteína.

Objetivo del estudio:

Para caracterizar el complejo de hierro (II) del Pseudomonas aeruginosa azurin apoprotein.
Investigar el entorno de coordinación y las propiedades electrónicas del hierro enlazado (II).
Para explorar el efecto de las mutaciones en la unión de aniones con el hierro (II) centro.

Principales métodos:

La espectroscopia de absorción electrónica es una espectroscopia de absorción electrónica.
La espectroscopia Mössbauer es una espectroscopia de Mössbauer.
La espectroscopia de resonancia magnética nuclear (RMN) también se conoce como espectroscopia de resonancia magnética nuclear.
Cristalografía de rayos X con rayos X.
Cálculos cuántico-químicos de las computaciones.
Mutagénesis dirigida al sitio.

Principales resultados:

El hierro (II) forma un complejo estable 1:1 con la apoproteína azurina de Pseudomonas aeruginosa.
El ión hierro (II) está estrechamente unido en un entorno pseudotetraédrico de baja coordenada que involucra a His, Cys y Gly45.
El complejo de hierro (II) es redox-inactivo.
Los cálculos químicos cuánticos revelan un estado de hierro (II) de alto espín con un orbital d (z2) doblemente ocupado.
La mutación de Met121 a Ala crea una bolsa para la unión de aniones reversibles (por ejemplo, azido, cianuro).
La unión de azido da como resultado un complejo de hierro de alto espín (II), mientras que la unión de cianuro da como resultado un complejo de hierro de bajo espín (II).

Conclusiones:

La apoproteína de Pseudomonas aeruginosa azurin puede unirse al hierro en un entorno de coordinación único.
Las propiedades electrónicas y estructurales del complejo de hierro (II) sugieren un estado estable, redox-inactivo.
El mutante Met121Ala diseñado demuestra el potencial para modular las propiedades del sitio del metal e introducir capacidades de unión de aniones.

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