Optimization of Electrochemical and Peroxide‐Driven Oxidation of Styrene with Ultrathin Polyion Films Containing Cytochrome P450cam and Myoglobin

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Abstract
The catalytic and electrochemical properties of myoglobin and cytochrome P450camin films constructed with alternate polyion layers were optimized with respect to film thickness, polyion type, and pH. Electrochemical and hydrogen peroxide driven epoxidation of styrene catalyzed by the proteins was used as the test reaction. Ionic synthetic organic polymers such as poly(styrene sulfonate), as opposed to SiO2nanoparticles or DNA, supported the best catalytic and electrochemical performance. Charge transport involving the iron heme proteins was achieved over 40–320 nm depending on the polyion material and is likely to involve electron hopping facilitated by extensive interlayer mixing. However, very thin films (ca. 12–25 nm) gave the largest turnover rates for the catalytic epoxidation of styrene, and thicker films were subject to reactant transport limitations. Classical bell‐shaped activity/pH profiles and turnover rates similar to those obtained in solution suggest that films grown layer‐by‐layer are applicable to turnover rate studies of enzymes for organic oxidations. Major advantages include enhanced enzyme stability and the tiny amount of protein required.