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Ferrocyanide‐Mediated Photoreduction of Ferricytochrome C Utilized to Selectively Probe Non‐native Conformations Induced by Binding to Cardiolipin‐Containing Liposomes
Author(s) -
Malyshka Dmitry,
SchweitzerStenner Reinhard
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201604992
Subject(s) - liposome , cardiolipin , cytochrome c , chemistry , native state , potassium ferrocyanide , biophysics , raman spectroscopy , population , biochemistry , membrane , biology , mitochondrion , phospholipid , organic chemistry , physics , demography , sociology , optics
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.