Thermodynamic aspects of the adsorption of cytochrome c and its mutants on kaolinite

The adsorption of native, wild-type, and engineered cytochrome c on sodium-exchanged kaolinite was investigated by spectroscopic means. The variants of yeast cytochrome c were obtained replacing surface lysines in positions 72, 73, and 79 with alanine residues. All proteins are strongly adsorbed ont...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 12 vom: 16. Juni, Seite 6849-55
1. Verfasser: Castellini, Elena (VerfasserIn)
Weitere Verfasser: Ranieri, Antonio, Simari, Domenico A, Di Rocco, Giulia
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Kaolin 24H4NWX5CO Cytochromes c 9007-43-6
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520 |a The adsorption of native, wild-type, and engineered cytochrome c on sodium-exchanged kaolinite was investigated by spectroscopic means. The variants of yeast cytochrome c were obtained replacing surface lysines in positions 72, 73, and 79 with alanine residues. All proteins are strongly adsorbed onto kaolinite. In particular, the presence of the lysine residue in position 73 remarkably favors adsorption. A detailed characterization of the thermodynamic aspects of the adsorption process has been performed. Most notably, adsorbed cytochrome c maintains its moderate peroxidase activity against guaiacol. This investigation is prodromal to the exploitation of the catalytic activity of engineered cytochrome c immobilized on a polydisperse system 
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700 1 |a Ranieri, Antonio  |e verfasserin  |4 aut 
700 1 |a Simari, Domenico A  |e verfasserin  |4 aut 
700 1 |a Di Rocco, Giulia  |e verfasserin  |4 aut 
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