Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids

Andreas Ioannis Karsisiotis, Oliver M. Deacon, Colin Macdonald, Tharin M. A. Blumenschein, Geoffrey R. Moore, Jonathan A. R. Worrall

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Human cytochrome c plays a central role in the mitochondrial electron transfer chain and in the intrinsic apoptosis pathway. Through the interaction with the phospholipid cardiolipin, cytochrome c triggers release of pro-apoptotic factors, including itself, from the mitochondrion into the cytosol of cells undergoing apoptosis. The cytochrome c/cardiolipin complex has been extensively studied through various spectroscopies, most recently with high-field solution and solid-state NMR spectroscopies, but there is no agreement between the various studies on key structural features of cytochrome c in its complex with cardiolipin. In the present study, we report backbone 1H, 13C, 15N resonance assignments of acid-denatured human cytochrome c in the aprotic solvent dimethylsulfoxide. These have led to the assignment of a reference 2D 1H-15N HSQC spectrum in which out of the 99 non-proline residues 87% of the backbone amides are assigned. These assignments are being used in an interrupted H/D exchange strategy to map the binding site of cardiolipin on human cytochrome c.
Original languageEnglish
Pages (from-to)165–168
Number of pages4
JournalBiomolecular NMR Assignments
Issue number2
Early online date4 Mar 2017
Publication statusPublished - Oct 2017


  • human cytochrome c
  • apoptosis
  • cardiolipin
  • acid-denatured
  • DMSO

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