Relationships between bilayer lipid, motional freedom of oxidoreductase components, and electron transfer in the mitochondrial inner membrane.

Abstract:

:The relationships between bilayer lipid, diffusional and conformational activities of oxidoreduction components, and electron transfer activity in the mitochondrial inner membrane are considered. Using a new, low pH method to fuse liposome phospholipid (asolectin) with the isolated mitochondrial inner membrane, the membrane bilayer is enriched up to 700% with exogenous phospholipid. During such enrichment, ultrastructural analysis reveals that integral proteins diffuse freely and randomly into the expanding bilayer. Kinetic analysis reveals that a diffusion limited step occurs between succinate- and NADH dehydrogenase and cytochromes bc1, and that the dehydrogenases, ubiquinone, and cytochromes bc1 are free to diffuse independently of one another in the membrane plane. Whether cytochromes bc1 and cytochrome c oxidase codiffuse in the membrane plane, or diffuse independently of one another remains unclear. The specific activities of succinate- and NADH-dehydrogenase as well as cytochrome c oxidase are affected by bilayer enrichment. This most likely occurs through the direct modulation by the newly incorporated phospholipid on conformational activity required in the oxidoreductases for electron transfer.

journal_name

Adv Exp Med Biol

authors

Hackenbrock CR,Schneider H,Lemasters JJ,Höchli M

doi

10.1007/978-1-4757-1419-7_26

subject

Has Abstract

pub_date

1980-01-01 00:00:00

pages

245-63

eissn

0065-2598

issn

2214-8019

journal_volume

132

pub_type

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