The NH2-terminal region of rabbit CYP2E1 is not essential for interaction with NADPH-cytochrome P450 reductase.
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.
Voznesensky
A I
AI
Department of Pharmacology, University of Connecticut Health Center, Farmington 06030-1505.
Schenkman
J B
JB
Pernecky
S J
SJ
Coon
M J
MJ
D000818:Animals; D019392:Cytochrome P-450 CYP2E1; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D009994:Osmolar Concentration; D010084:Oxidation-Reduction; D010089:Oxidoreductases, N-Demethylating / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010446:Peptide Fragments; D011817:Rabbits
D010446:Peptide Fragments; D003577:Cytochrome P-450 Enzyme System; D019392:Cytochrome P-450 CYP2E1; D010089:Oxidoreductases, N-Demethylating; D009251:NADPH-Ferrihemoprotein Reductase