How the Local Geometry of the Cu-Binding Site Determines the Thermal Stability of Blue Copper Proteins
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...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión enviada para evaluación y publicación |
| Fecha de publicación: | 2011 |
| País: | España |
| Institución: | Universidad de Sevilla (US) |
| Repositorio: | idUS. Depósito de Investigación de la Universidad de Sevilla |
| OAI Identifier: | oai:idus.us.es:11441/66489 |
| Acceso en línea: | http://hdl.handle.net/11441/66489 https://doi.org/10.1016/j.chembiol.2010.12.006 |
| Access Level: | acceso abierto |
| Palabra clave: | Cupredoxin Enzymes Biotechnological application Plastocyanin Synechocystis Phormidium Cyanobacteria |
| Sumario: | 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. |
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