Recently we reported that electrostatic forces interfere with the formation of the NADPH-cytochrome P450 reductase/cytochrome P450 electron transfer complex and suggested that this complex is formed by the attraction of the complementary hydrophobic patches (Voznesensky, A., and Schenkman,J.(1994) 269 J.Biol.Chem, 15724-1573). In this report we evaluate the role of the NH2-terminal hydrophobic region of CYP2E1 in the interaction with the reductase by comparing ionic strength dependence of the reduction of the full-length and truncated [Delta]3-29 CYP2E1. Increasing ionic strength stimulates reduction of both full-length and truncated CYP2E1. The neutralization of electrostatic interactions by increasing ionic strength revealed no impairment of the [Delta]3-29 CYP2E1 reduction compared to that of the full-length CYP2E1, indicating that the NH2-terminal region is not essential for the interaction of the cytochrome with the reductase
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