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Ferrocyanide-Mediated Photoreduction of Ferricytochrome C Utilized to Selectively Probe Non-native Conformations Induced by Binding to Cardiolipin-Containing Liposomes
Journal article

Ferrocyanide-Mediated Photoreduction of Ferricytochrome C Utilized to Selectively Probe Non-native Conformations Induced by Binding to Cardiolipin-Containing Liposomes

Dmitry Malyshka and Reinhard Schweitzer-Stenner
Chemistry : a European journal, v 23(5), pp 1151-1156
01 Jan 2017
PMID: 27859757

Abstract

Chemistry Chemistry, Multidisciplinary Physical Sciences Science & Technology
Ferricytochrome c binding to cardiolipin-containing liposomes produces a heterogeneous distribution of conformations comprising native-like and non-native misfolded proteins. We utilized the photoreduction of native ferricytochrome c in the presence of potassium ferrocyanide and resonance Raman spectroscopy to probe the population of native and misfolded cytochrome c on liposomes with 20% tetraoleylcardiolipin (TOCL)/80% dioleylphosphocholine (DOPC) and with 100% TOCL as a function of TOCL concentration. Our data provided strong support for an earlier model, which predicts that the equilibrium between native and non-native conformations is shifted to the latter with decreasing protein occupation of liposomes.

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Web of Science research areas
Chemistry, Multidisciplinary
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