Spectroelectrochemical measurements of redox proteins by using a simple UV/visible cell

• We provide details of a UV/Vis cell for spectroelectrochemical measurements.
• This cell does not require high sample concentrations as the OTTLE cell.
• We report the spectroelectrochemical studies of various redox proteins.
• We studied cytochrome c, myoglobin, horseradish peroxidase, and cytochrome bc1.
• The measured midpoint potentials of these proteins agree with their literature values.

Details are provided of a spectroelectrochemical cell that consists of a UV/vis cuvette. We report the UV/vis spectroelectrochemical measurements of cytochrome c, myoglobin, horseradish peroxidase, and cytochrome bc1 at pH 7.0. The application on cytochrome c was performed by direct electron exchange between the protein and the working electrode. On the other hand, the measurements on myoglobin, horseradish peroxidase, and cytochrome bc1 were carried out in the presence of redox mediators. All the proteins display one-electron redox changes, as expected and measured midpoint potentials (Em) that agree with previously reported values.

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