Enhancing Biocatalysis: The Case of Unfolded Cytochrome c Immobilized on Kaolinite. Issue 7 (5th April 2013)

• Record Type: Journal Article
• Authors: Castellini, Elena; Bortolotti, Carlo Augusto; Di Rocco, Giulia; Bernini, Fabrizio; Ranieri, Antonio
• Is Part Of: ChemCatChem. Volume 5:Issue 7(2013:Jul.)
• Page Start: 1765
• Page End: 1768
• Publication Date: 2013-04-05
• Subjects: Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201200876
• Languages: English
• ISSNs: 1867-3880

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Enhanced catalysis!</bold> Urea‐unfolded wild‐type cytochrome <italic>c</italic> 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg22f4zxjx" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>