Artículo
How the Local Geometry of the Cu-Binding Site Determines the Thermal Stability of Blue Copper Proteins
Autor/es | Chaboy, Jesús
Díaz Moreno, Sofía Díaz Moreno, Irene Rosa Acosta, Miguel Ángel de la Díaz Quintana, Antonio Jesús |
Departamento | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Fecha de publicación | 2011-01 |
Fecha de depósito | 2017-11-22 |
Publicado en |
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Resumen | Identifying the factors that govern the thermal resistance of cupredoxins is essential for understanding their folding and stability, and for improving our ability to design highly stable enzymes with potential biotechnological ... Identifying the factors that govern the thermal resistance of cupredoxins is essential for understanding their folding and stability, and for improving our ability to design highly stable enzymes with potential biotechnological applications. Here, we show that the thermal unfolding of plastocyanins from two cyanobacteria—the mesophilic Synechocystis and the thermophilic Phormidium—is closely related to the short-range structure around the copper center. Cu K-edge X-ray absorption spectroscopy shows that the bond length between Cu and the S atom from the cysteine ligand is a key structural factor that correlates with the thermal stability of the cupredoxins in both oxidized and reduced states. These findings were confirmed by an additional study of a site-directed mutant of Phormidium plastocyanin showing a reverse effect of the redox state on the thermal stability of the protein. |
Agencias financiadoras | Ministerio de Ciencia e Innovación (MICIN). España Junta de Andalucía |
Identificador del proyecto | CICYT-MAT2008-06542-C04
BFU2009-07190 BIO-198 P06-CVI-01713 |
Cita | Chaboy, J., Díaz Moreno, S., Díaz Moreno, I., De la Rosa Acosta, M.Á. y Díaz Quintana, A. (2011). How the Local Geometry of the Cu-Binding Site Determines the Thermal Stability of Blue Copper Proteins. Chemistry and Biology, 18 (1), 25-31. |
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