Abstract
The structural changes in cytochrome c with temperature have been been followed using a recently developed electrically-heated microelectrode sensor. Differential pulse voltammetry was used to perform electrochemical measurements of cytochrome c oxidation at different temperatures at heated bare gold electrodes contained in phosphate-buffered cytochrome c solution at room temperature. The voltammetric response shows the onset of unfolding and a marked dependence of the signal on electrode temperature. This augurs well for applications of heated electrodes as local probes in the study of the temperature dependence of electron transfer processes of other redox proteins, avoiding problems of bulk deterioration.
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