Projects per year
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.
- human cytochrome c
- 1 Finished
- 1 Article
Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic ActivityDeacon, 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
Research output: Contribution to journal › ArticleOpen AccessFile24 Citations (Scopus)12 Downloads (Pure)