Single-molecule in vivo imaging of bacterial respiratory complexes indicates delocalized oxidative phosphorylation


Llortente-Garcia, I, Lenn, T, Erhardt, H, Harriman, O, Liu, LN ORCID: 0000-0002-8884-4819, Robson, A, Chiu, SW, Matthews, S, Willis, N, Bray, C et al (show 7 more authors) (2014) Single-molecule in vivo imaging of bacterial respiratory complexes indicates delocalized oxidative phosphorylation. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1837 (6). pp. 811-824.

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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 100–200 nm 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.

Item Type: Article
Additional Information: ## TULIP Type: Articles/Papers (Journal) ##
Uncontrolled Keywords: Cytoplasmic membrane, Co-localization analysis, Fluorescence microscopy, Fluorescent protein, Oxidative phosphorylation, Single-molecule biophysics
Depositing User: Symplectic Admin
Date Deposited: 25 Apr 2016 14:39
Last Modified: 21 Jan 2023 01:43
DOI: 10.1016/j.bbabio.2014.01.020
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3000553
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