How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing |
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Authors: | Antonio Ranieri Marco Borsari Stefano Casalini Giulia Di Rocco Marco Sola Carlo Augusto Bortolotti Gianantonio Battistuzzi |
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Affiliation: | 1.Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125 Modena, Italy; (A.R.); (G.D.R.); (M.S.);2.Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125 Modena, Italy;3.Department of Chemical Sciences, University of Padova, Via Marzolo 1, 35131 Padova, Italy; |
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Abstract: | Cytochrome c is a small globular protein whose main physiological role is to shuttle electrons within the mitochondrial electron transport chain. This protein has been widely investigated, especially as a paradigmatic system for understanding the fundamental aspects of biological electron transfer and protein folding. Nevertheless, cytochrome c can also be endowed with a non-native catalytic activity and be immobilized on an electrode surface for the development of third generation biosensors. Here, an overview is offered of the most significant examples of such a functional transformation, carried out by either point mutation(s) or controlled unfolding. The latter can be induced chemically or upon protein immobilization on hydrophobic self-assembled monolayers. We critically discuss the potential held by these systems as core constituents of amperometric biosensors, along with the issues that need to be addressed to optimize their applicability and response. |
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Keywords: | redox biosensing cytochrome c surface immobilization |
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