Apparent Dependence of Interactions Between Cytochrome B5 and Cytochrome B5 Reductase Upon Translational Diffusion in Dimyristoyl Lecithin Liposomes

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1975 Jul 1

PMID 1058480

Citations 19

Authors

P STRITTMATTER

M J Rogers

Affiliations

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Abstract

Dimyristoyl lecithin liposomes, containing cytochrome b5 reductase (NADH:ferricytochrome b5 oxidoreductase, EC 1.6.2.2) and varying amounts of cytochrome b5, were used to measure flavoprotein catalysis alone and catalysis requiring electron transfer between the reductase and cytochrome as a function of temperature. Whereas flavoprotein catalysis showed a simple linear temperature dependence in an Arrhenius plot, the reaction involving electron transfer between the two bound enzymes showed a marked, 4-fold, change in rate at the crystalline-liquid crystalline phase transition of the hydrocarbon chains of the lecithin vesicles and a second, minor change involving the minor transition. These data represent strong evidence that protein-protein interactions in this membrane model system are dependent upon translational diffusion of nonpolar segments of the proteins in the hydrocarbon region of the phospholipid bilayer.

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