Projects per year
Abstract
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 language | English |
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Pages (from-to) | 165–168 |
Number of pages | 4 |
Journal | Biomolecular NMR Assignments |
Volume | 11 |
Issue number | 2 |
Early online date | 4 Mar 2017 |
DOIs | |
Publication status | Published - Oct 2017 |
Keywords
- human cytochrome c
- apoptosis
- cardiolipin
- acid-denatured
- DMSO
Projects
- 1 Finished
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Fat(al) attraction of cytochrome c: A new approach to study protein-lipid interactions
1/02/14 → 31/01/17
Project: Research
Research output
- 2 Citations (Scopus)
- 1 Article
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Heightened dynamics of the oxidized Y48H variant of human cytochrome c increases its peroxidatic activity
Deacon, O., Karsisiotis, A. I., Moreno-Chicano, T., Hough, MA., Macdonald, C., Blumenschein, T. M. A., Wilson, M. T., Moore, G. R. & Worrall, JA. R., 21 Nov 2017, In: Biochemistry. 56, 46, p. 6111–6124 14 p.Research output: Contribution to journal › Article › peer-review
Open AccessFile41 Citations (SciVal)19 Downloads (Pure)