AI Article Synopsis
- Researchers reconstituted cytochrome c oxidase in phospholipid vesicles with hydrophobic poly(vinyl alkanoate) polymers, resulting in smaller vesicle diameters compared to standard proteoliposomes.
- Electron microscopy confirmed that this polymer interaction maintained the protein's orientation in the membrane and preserved respiratory control during enzyme function.
- Additionally, the study found a relationship between vesicle size and respiratory control ratio, supporting earlier models of cytochrome c oxidase activity regulation.
Article Abstract
Cytochrome c oxidase was reconstituted in phospholipid vesicles in the presence of highly hydrophobic poly(vinyl alkanoate) polymers. Electron-microscopy observations demonstrated that polymer interaction with the lipid phase induces vesicles to adopt smaller diameters than those typical of standard proteoliposomes. Functional characterization of these polymer-proteoliposome structures indicates that the reconstitution of the enzyme proceeds efficiently without causing either scrambling of the protein orientation in the membrane or loss of respiratory control. A clear dependence of respiratory control ratio on vesicle size was also demonstrated, which is in agreement with a previous model proposed for control of activity of cytochrome c oxidase vesicles [Brunori, Sarti, Colosimo, Antonini, Malatesta, Jones & Wilson (1985) EMBO J. 4, 2365-2368].
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1135656 | PMC |
| http://dx.doi.org/10.1042/bj2570783 | DOI Listing |
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