In this section
Some of the covers featuring our work are shown below:
Wilton-Ely J, 2006, Dinuclear ruthenium and osmium compounds with metal-metal bonds, Comprehensive Organometallic Chemistry III, Editor(s): Crabtree, Mingos, Elsevier, Pages:647-716, ISBN:978-0080445908
@article{Eisermann:2023:10.1039/d2cb00158f,
author = {Eisermann, J and Wright, JJ and Wilton-Ely, JDET and Hirst, J and Roessler, MM},
doi = {10.1039/d2cb00158f},
journal = {RSC Chemical Biology},
pages = {386--398},
title = {Using light scattering to assess how phospholipid-protein interactions affect complex I functionality in liposomes},
url = {http://dx.doi.org/10.1039/d2cb00158f},
volume = {4},
year = {2023}
}
TY - JOUR
AB - Complex I is an essential membrane protein in respiration, oxidising NADH and reducing ubiquinone to contribute to the proton-motive force that powers ATP synthesis. Liposomes provide an attractive platform to investigate complex I in a phospholipid membrane with the native hydrophobic ubiquinone substrate and proton transport across the membrane, but without convoluting contributions from other proteins present in the native mitochondrial inner membrane. Here, we use dynamic and electrophoretic light scattering techniques (DLS and ELS) to show how physical parameters, in particular the zeta potential (ζ-potential), correlate strongly with the biochemical functionality of complex I-containing proteoliposomes. We find that cardiolipin plays a crucial role in the reconstitution and functioning of complex I and that, as a highly charged lipid, it acts as a sensitive reporter on the biochemical competence of proteoliposomes in ELS measurements. We show that the change in ζ-potential between liposomes and proteoliposomes correlates linearly with protein retention and catalytic oxidoreduction activity of complex I. These correlations are dependent on the presence of cardiolipin, but are otherwise independent of the liposome lipid composition. Moreover, changes in the ζ-potential are sensitive to the proton motive force established upon proton pumping by complex I, thereby constituting a complementary technique to established biochemical assays. ELS measurements may thus serve as a more widely useful tool to investigate membrane proteins in lipid systems, especially those that contain charged lipids.
AU - Eisermann,J
AU - Wright,JJ
AU - Wilton-Ely,JDET
AU - Hirst,J
AU - Roessler,MM
DO - 10.1039/d2cb00158f
EP - 398
PY - 2023///
SN - 2633-0679
SP - 386
TI - Using light scattering to assess how phospholipid-protein interactions affect complex I functionality in liposomes
T2 - RSC Chemical Biology
UR - http://dx.doi.org/10.1039/d2cb00158f
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000959176500001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=a2bf6146997ec60c407a63945d4e92bb
UR - https://pubs.rsc.org/en/content/articlelanding/2023/CB/D2CB00158F
UR - http://hdl.handle.net/10044/1/104155
VL - 4
ER -