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

DOI: 10.1016/j.chembiol.2010.12.006 DOI Help

Authors: Jesus Chaboy (University of Zaragoza) , Sofia Diaz-moreno (Diamond Light Source) , I. Diaz-moreno (Consejo Superior de Investigaciones Científicas-Universidad de Sevilla) , Miguel A. De La Rosa (Consejo Superior de Investigaciones Científicas-Universidad de Sevilla) , Antonio Diaz-quintana (Consejo Superior de Investigaciones Científicas-Universidad de Sevilla)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chemistry & Biology , VOL 18 (1) , PAGES 25-31

State: Published (Approved)
Published: January 2011

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.

Subject Areas: Chemistry, Biology and Bio-materials


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Added On: 16/03/2011 09:48

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