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Interaction of lutein with mitochondrial and artificial membranes

Chaturvedi, VK and Kurup, Ramakrishna CK (1987) Interaction of lutein with mitochondrial and artificial membranes. [Book Chapter]

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Abstract

Addition of intact chloroplasts to mitochondria resulted in the uncoupling and inhibition of oxidative phosphorylation. The uncoupling principle was identified as the xanthophyll lutein. The oxidation of NADH was more sensitive to inhibition by lutein than was the oxidation of succinate or ascorbate. Xanthophyll stimulated the ATPase activity of mitochondria in the presence of $Mg^{2+}$; in the absence of $Mg^{2+}$, it inhibited the enzyme activity. Differential calorimetric scans revealed that incorporation of lutein into aq. dispersions of dipalmitoyl phosphatidyl choline decreased the transition enthalpy as well as the size of the cooperative unit, without change in the temp. of transition. Permeability of the bilayer to ascorbate and $Ca^{2+}$ was enhanced significantly in the presence of lutein. The efflux of $Ca^{2+}$ from mitochondria was enhanced. Incorporation of the xanthophyll broadened NMR peaks of both acyl side chain methylene and terminal Me protons without change in the line width of the choline head group Me proton signal. These results reveal that the deleterious action of lutein on mitochondrial oxidative phosphorylation results from its ability to integrate deep into the hydrophobic regions of the bilayer and perturb the microenvironment.

Item Type: Book Chapter
Additional Information: Copyright of this article belongs to Today & Tomorrow's Printers & Publishers.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 14 Mar 2008
Last Modified: 27 Aug 2008 13:14
URI: http://eprints.iisc.ernet.in/id/eprint/13276

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