Global analysis of protein-protein interactions reveals multiple CYP2E1-reductase complexes.

ABSTRACT: Although a single binary functional complex between cytochrome P450 (P450 or CYP for a specific isoform) and cytochrome P450 reductase (CPR) has been generally accepted in the literature, this simple model failed to explain the experimentally observed catalytic activity of recombinant CYP2E1 in dependence on the total concentration of the added CPR-K56Q mutant. Our rejection of the simplest 1:1 binding model was based on two independent lines of experimental evidence. First, under the assumption of the 1:1 binding model, separate analyses of titration curves obtained while varying either P450 or CPR concentrations individually produced contradictory results. Second, an asymmetric Job plot suggested the existence of higher order molecular complexes. To identify the most probable complexatio

SUBMITTER: Jamakhandi AP 

PROVIDER: S-EPMC2592557 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature