Membrane binding induces destabilization of cytochrome c structure

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DOIResolve DOI: http://doi.org/10.1021/bi00243a025
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TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume30
Issue29
Pages72197224
AbstractThe effect of membrane binding on the structure and stability of ferricytochrome c was studied by Fourier-transform infrared spectoscopy and differential scanning calorimetry. Association of cytochrom c with phospholipid membranes containing phosphatidylglycerol as a model acidic phospholipid results in only slight, if any, perturbation of the protein secondary nature. However, upon membrane binding, there is a considerable increase in the accessibility of protein backbone amide groups to hydrogen-deuterium exchange, which suggests a lipid-mediated loosening and/or destabilization o fthe protein tertiary structure. A lipid-induced conformational perturbation of ferricytochrome c is also indicated by a marked decrease in the thermodynamic stability of the membrane-bound protein. Upon binding to the membranes containing dimyristoylphosphatidyglycerol (DMPG) or dioleoylphosphatidylglycerol (DOPG) as a single lipid component, the denaturation temperature of ferricytochrome c decreases by approximately 30⁰C. This is accompanied by a decrease in the calorimetric enthalpy of denaturation, patricularly for the DMPG-associated protein. With ferricytochrome c bound to membranes containing a mixture of DMPG (DOPG) and zwitterionic phosphatidylcholine, the extent of structural perturbation depends on the surface density of the negatively charged lipid head groups, becoming smaller with decreasing proportions of acidic phospholipid in the membrane. The observed destabilization of protein structure mediated by acidic phospholipids (and possibly formation of folding intermediates at the membrane surface) may represent a general property of a larger class of water-soluble proteins for which membrane binding is governed by electrostatic forces.
Publication date
LanguageEnglish
AffiliationNRC Steacie Institute for Molecular Sciences; NRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NRC number32300
NPARC number23001457
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Record identifierb7c8efdf-3805-44d7-8724-c8cf0941e62f
Record created2017-02-13
Record modified2017-02-14
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