Publication | Open Access
Cytochrome P-450scc-phospholipid interactions. Evidence for a cardiolipin binding site and thermodynamics of enzyme interactions with cardiolipin, cholesterol, and adrenodoxin.
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Citations
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References
1983
Year
Proteinlipid InteractionAldo-keto ReductaseLipid PeroxidationCytochrome P-450scc-phospholipid InteractionsRedox BiologyOxidative StressEnzyme InteractionsMolecular PharmacologyHealth SciencesHydrophobic MembraneMolecular PhysiologyOxysterolBiochemistryCytochrome P-450Membrane BiologyPharmacologyBiomolecular EngineeringPhysiologyLipoprotein MetabolismLipid ChemistryMedicineElectron Shuttle
function as an electron shuttle (3-5); adre- nodoxin in its complex with NADPH-reduced reductase fist accepts an electron from the reduced flavoprotein, then dis- sociates and forms a 1:l complex with cytochrome P-450, and finally transfers an electron to the hemoprotein. Cholesterol binds to the cytochrome via the hydrophobic membrane in which this substrate
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