Apparent dependence of interactions between cytochrome b5 and cytochrome b5 reductase upon translational diffusion in dimyristoyl lecithin liposomes.

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.

authors

Strittmatter P,Rogers MJ

doi

10.1073/pnas.72.7.2658

keywords:

subject

Has Abstract

pub_date

1975-07-01 00:00:00

pages

2658-61

issue

7

eissn

0027-8424

issn

1091-6490

journal_volume

72

pub_type

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