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How the Local Geometry of the Cu-Binding Site Determines the Thermal Stability of Blue Copper Proteins

 

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Opened Access How the Local Geometry of the Cu-Binding Site Determines the Thermal Stability of Blue Copper Proteins
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Author: Chaboy, Jesús
Díaz Moreno, Sofía
Díaz Moreno, Irene
Rosa Acosta, Miguel Ángel de la
Díaz Quintana, Antonio Jesús
Department: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Date: 2011-01
Published in: Chemistry and Biology, 18 (1), 25-31.
Document type: Article
Abstract: 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.
Cite: 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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URI: http://hdl.handle.net/11441/66489

DOI: 10.1016/j.chembiol.2010.12.006

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