Llorente-Garcia, Isabel, Lenn, Tchern, Erhardt, Heiko et al. (14 more authors) (2014) Single-molecule in vivo imaging of bacterial respiratory complexes indicates delocalized oxidative phosphorylation. Biochimica et Biophysica Acta. Bioenergetics. pp. 811-824. ISSN 0005-2728
Abstract
Chemiosmotic energy coupling through oxidative phosphorylation (OXPHOS) is crucial to life, requiring coordinated enzymes whose membrane organization and dynamics are poorly understood. We quantitatively explore localization, stoichiometry, and dynamics of key OXPHOS complexes, functionally fluorescent protein-tagged, in Escherichia coli using low-angle fluorescence and superresolution microscopy, applying single-molecule analysis and novel nanoscale co-localization measurements. Mobile 100-200nm membrane domains containing tens to hundreds of complexes are indicated. Central to our results is that domains of different functional OXPHOS complexes do not co-localize, but ubiquinone diffusion in the membrane is rapid and long-range, consistent with a mobile carrier shuttling electrons between islands of different complexes. Our results categorically demonstrate that electron transport and proton circuitry in this model bacterium are spatially delocalized over the cell membrane, in stark contrast to mitochondrial bioenergetic supercomplexes. Different organisms use radically different strategies for OXPHOS membrane organization, likely depending on the stability of their environment.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2014 The Authors. Published by Elsevier B.V. This is an open access article under a Creative Commons Attribution (CC BY) licence. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) The University of York > Faculty of Sciences (York) > Physics (York) |
Depositing User: | Pure (York) |
Date Deposited: | 05 Mar 2015 13:02 |
Last Modified: | 16 Oct 2024 12:24 |
Published Version: | https://doi.org/10.1016/j.bbabio.2014.01.020 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.bbabio.2014.01.020 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:83995 |
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