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

Karsisiotis, Andreas Ioannis, Deacon, Oliver M., Macdonald, Colin, Blumenschein, Tharin M. A. ORCID: https://orcid.org/0000-0002-4932-5178, Moore, Geoffrey R. and Worrall, Jonathan A. R. (2017) Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids. Biomolecular NMR Assignments, 11 (2). 165–168. ISSN 1874-2718

Preview

PDF (Accepted manuscript) - Accepted Version Download (290kB) | Preview

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.

Item Type:	Article
Uncontrolled Keywords:	human cytochrome c,apoptosis,cardiolipin,acid-denatured,dmso
Faculty \ School:	Faculty of Science Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Depositing User:	Pure Connector
Date Deposited:	04 Mar 2017 01:41
Last Modified:	01 Oct 2024 01:46
URI:	https://ueaeprints.uea.ac.uk/id/eprint/62851
DOI:	10.1007/s12104-017-9740-0

Downloads

Actions (login required)

View Item