Increase of the peroxidase activity of cytochrome c-550 by the interaction with detergents

Abstract

The effect was studied of detergents on the peroxidase activity of the heme-containing electron-transport protein, cytochrome c-550 from Paracoccus versutus (cytc550). Cytc550 does not interact with non-ionic or zwitterionic detergents, but its peroxidase activity is significantly enhanced in the presence of both anionic and cationic detergents. The increase in peroxidase activity is caused by (partial) unfolding of cytc550, resulting in weakening of the bond between the axial methionine ligand and the heme-iron. With sodium dodecyl sulfate (SDS) and dodecyltrimethylammonium bromide (DTAB), the activity increases roughly 10- and 100-fold, respectively. The detergent concentration required to enhance the peroxidase activity of cytc550 consistently coincides with the critical micellisation concentration (CMC). When cytc550 carries substantial opposite charge to that of the detergent headgroup, the protein–detergent complex is formed at lower detergent concentration than the critical micellisation concentration, i.e. at acid pH for anionic detergent and at alkaline pH for cationic detergent. It is concluded that in the presence of ionic detergents, cytc550 can acquire considerable peroxidase activity. This may be exploited by applying cytc550 as an oxidative catalyst in detergent-rich environments, where regular peroxidases rapidly lose their catalytic potential.