Publication | Open Access
Violaxanthin De-Epoxidase, the Xanthophyll Cycle Enzyme, Requires Lipid Inverted Hexagonal Structures for Its Activity
117
Citations
12
References
2004
Year
Proteinlipid InteractionBilayer-forming LipidsHexagonal StructuresEngineeringMolecular BiologyLipid MovementChemical BiologyEnzymatic ModificationRedox BiologyFatty AcidsStructure-function Enzyme KineticsBiochemistryLipid ResourceLipidsBiomolecular EngineeringCellular EnzymologyXanthophyll Cycle EnzymeNatural SciencesViolaxanthin De-epoxidase
Bilayer-forming lipids were shown to be ineffective in sustaining the enzymatic activity of violaxanthin de-epoxidase. On the other hand, non-bilayer-forming lipids, regardless of their different chemical character, ensured high activity of violaxanthin de-epoxidase, resulting in conversion of violaxanthin to zeaxanthin. Our data indicates that the presence of lipids forming reversed hexagonal structures is necessary for violaxanthin de-epoxidase activity and this activity is dependent on the degree of unsaturation of the fatty acids. The significance of the reversed hexagonal phase domains in the conversion of violaxanthin into zeaxanthin in model systems and in the native thylakoid membranes is discussed.
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