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Rotation and interaction with epoxide hydrase of cytochrome P-450 in proteoliposomes. by H.U. Etter; C. Richter; Y. Ohta; K.H. Winterhalter; H. Sasabe; S. Kawato is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Purified rat liver cytochrome P-450MC or P-450PB was co-reconstituted with epoxide hydrase in liposomal vesicles made of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine at a lipid to protein weight ratio of 5 by the cholate dialysis procedure. Rotational diffusion of the cytochromes was measured by observing the decay of absorption anisotropy, r(t), after photolysis of the heme.CO complex by a vertically polarized laser flash. Analysis of r(t) was based on a "rotation-about-membrane-normal" model. The measurements were used to investigate interactions of cytochrome P-450MC or P-450PB with epoxide hydrase. Different rotational mobilities of the two cytochromes were observed. The amount of mobile molecules was 78% for cytochrome P-450MC and 91% for P-450PB, and the rest was immobile within the experimental time range of 1 ms. In the presence of epoxide hydrase 85% of cytochrome P-450MC and 96% of P-450PB were mobile. Cross-linking of epoxide hydrase by anti-epoxide hydrase antibodies resulted in a drastic immobilization of the cytochromes, reducing the mobile population to 49% for P-450MC and to 60% for P-450PB. The rotational relaxation times phi of the mobile

Who reads Rotation and interaction with epoxide hydrase of cytochrome P-450 in proteoliposomes.?

Author

H.U. Etter; C. Richter; Y. Ohta; K.H. Winterhalter; H. Sasabe; S. Kawato

Publisher

Elsevier BV

Published

1991

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)