PMID: 6412745Jul 19, 1983Paper

Possible association of NADPH-cytochrome P-450 reductase and cytochrome P-450 in reconstituted phospholipid vesicles

Biochemistry
Y NisimotoY Shibata

Abstract

A fluorescent probe, N-(1-anilinonaphth-4-yl)-maleimide (ANM), was specifically labeled to SH group(s) in the hydrophilic moiety of NADPH-cytochrome P-450 reductase at a ratio of 1 +/- 0.1 ANM/mol of protein. The ANM-labeled reductase and P-450 were reconstituted in phosphatidylcholine-phosphatidylethanolamine-phosphatidylserine vesicles in which all of the enzymes were functionally active. The reconstitution of the mixed-function oxidase system was found to be strongly dependent on both the lipid to protein molar ratio and phospholipid composition. The interactions of ANM-labeled reductase with P-450 in proteoliposomes were investigated by perturbation of the fluorescence of ANM. Upon incorporation of P-450 into the phospholipids vesicles (ANM-reductase/P-450/lipids identical to 1:1.4:800), a significant decrease of total fluorescence intensity and slight increase of emission anisotropy of ANM were observed. In the average fluorescence lifetime of ANM bound with reductase, an appreciable change was shown between the absence and presence of P-450 in the vesicles. These data provide clear evidence that significant molecular interactions occur between the two proteins in a membranous reconstituted system.

References

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Citations

Jan 1, 1985·The International Journal of Biochemistry·A MomchilovaK Koumanov
Mar 1, 1988·Archives of Biochemistry and Biophysics·S G Nadler, H W Strobel
Sep 6, 2005·Biochemical and Biophysical Research Communications·Dorota A Kwaśnicka-Crawford, Steven R Vincent
Jan 14, 1986·Biochemical and Biophysical Research Communications·J J Lee, L S Kaminsky
Jun 17, 2006·Bioscience Reports·Ksenia N MyasoedovaNatalya N Magretova
Nov 1, 1989·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·J BlanckK Ruckpaul
Oct 1, 1984·Archives of Biochemistry and Biophysics·G T Miwa, A Y Lu

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