Urea-unfolded wild-type cytochrome c and its variants immobilized on kaolinite show peroxidase activity that is significantly higher than that of the folded wild-type protein. The accessibility of the substrate to the metal center and the influence of strategic amino acidic residues on the surface of the protein are discussed. This approach sheds light on the factors affecting the catalytic activity of a new versatile biocatalytic interface.
Enhancing Biocatalysis: The Case of Cytochrome c Unfolded Immobilized on Kaolinite / Castellini, Elena; Bortolotti, Carlo Augusto; DI ROCCO, Giulia; Bernini, Fabrizio; Ranieri, Antonio. - In: CHEMCATCHEM. - ISSN 1867-3880. - STAMPA. - 5:(2013), pp. 1765-1768. [10.1002/cctc.201200876]
Enhancing Biocatalysis: The Case of Cytochrome c Unfolded Immobilized on Kaolinite
CASTELLINI, Elena;BORTOLOTTI, Carlo Augusto;DI ROCCO, Giulia;BERNINI, FABRIZIO;RANIERI, Antonio
2013
Abstract
Urea-unfolded wild-type cytochrome c and its variants immobilized on kaolinite show peroxidase activity that is significantly higher than that of the folded wild-type protein. The accessibility of the substrate to the metal center and the influence of strategic amino acidic residues on the surface of the protein are discussed. This approach sheds light on the factors affecting the catalytic activity of a new versatile biocatalytic interface.
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