The Effect of Reactive Oxygen Species on Respiratory Complex I Activity in Liposomes.

Autor: Eisermann J; Department of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK.; Department of Chemistry, University of Stuttgart, Institute of Physical Chemistry, Pfaffenwaldring 55, 70569, Stuttgart, Germany., Liang Y; Department of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK., Wright JJ; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Building, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK., Clifford E; Department of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK., Wilton-Ely JDET; Department of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK., Kuimova MK; Department of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK., Roessler MM; Department of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK.
Jazyk: angličtina
Zdroj: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Oct 01; Vol. 30 (55), pp. e202402035. Date of Electronic Publication: 2024 Sep 17.
DOI: 10.1002/chem.202402035
Abstrakt: Respiratory complex I (R-CI) is an essential enzyme in the mitochondrial electron transport chain but also a major source of reactive oxygen species (ROS), which are implicated in neurodegenerative diseases and ageing. While the mechanism of ROS production by R-CI is well-established, the feedback of ROS on R-CI activity is poorly understood. Here, we perform EPR spectroscopy on R-CI incorporated in artificial membrane vesicles to reveal that ROS (particularly hydroxyl radicals) reduce R-CI activity by making the membrane more polar and by increasing its hydrogen bonding capability. Moreover, the mechanism that we have uncovered reveals that the feedback of ROS on R-CI activity via the membrane is transient and not permanent; lipid peroxidation is negligible for the levels of ROS generated under these conditions. Our successful use of modular proteoliposome systems in conjunction with EPR spectroscopy and other biophysical techniques is a powerful approach for investigating ROS effects on other membrane proteins.
(© 2024 The Author(s). Chemistry - A European Journal published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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