Observation of Fe(III) configurations of cytochrome c confined in mesoporous materials

Abstract

Proteins and enzymes immobilized in confined surroundings of mesoporous materials will develop their structures that are different from those of native solution states. In some cases, the enzymatic activity is shown to be improved when compared to the native solution state. Cytochrome c (cytc) can be used to catalyze the oxidation of some organic substrates in the presence of hydrogen peroxide, i.e. peroxidase-like activity. Immobilization of cytochrome c in mesoporous materials shows improvement of the peroxidase activity. The enhanced activity is reported to be related to the spin configuration of Fe(III) at the active site. In this review, the relationship of the Fe(III) configuration of cytc and the peroxidase activity is discussed. The knowledge on structure-activity of cytc is studied as a model for developing the bio-nano material composites providing better activity of the enzymes.