The optical biosensor method was used for the revelation of ternary complex
es, formed by the full-length NADPH-cytochrome P450 reductase (d-Fp) and cy
tochromes P4502B4 (d-2B4) and b5 (d-b5) in the course of their interactions
within the reconstituted d-2B4-containing system. Based on the lack of com
petition between d-b5 and d-Fp for the binding sites on immobilized 2B4 (3)
as well as on the analysis of data obtained in the three proteins' dissoci
ation reactions, the possibility of formation of ternary complexes through
the interactions between membranous hydrophobic fragments of proteins was s
ubstantiated. All the complexes obtained were productive. (C) 2000 Academic
Press.