Abstract
PSS as a representative conducting polymer, we compare a set of heme proteins (soybean peroxidase, cytochrome c, and horseradish peroxidase) used as oxidants. The resulting PSS was characterized with visible and near IR spectroscopy, Fourier transform infrared spectroscopy, electron spin resonance spectroscopy, and four point probe conductivity measurements. We find that the relative concentrations of bipolarons and polarons vary as a function of the protein used for polymerization. We then show that heme degradation by hydrogen peroxide plays a critical role in determining polymer properties.
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