Lenn, Tchern and Leake, Mark Christian orcid.org/0000-0002-1715-1249 (2016) Single-molecule studies of the dynamics and interactions of bacterial OXPHOS complexes. Biochimica et Biophysica Acta. Bioenergetics. pp. 224-231. ISSN 0005-2728
Abstract
Although significant insight has been gained into biochemical, genetic and structural features of oxidative phosphorylation (OXPHOS) at the single-enzyme level, relatively little was known of how the component complexes function together in time and space until recently. Several pioneering single-molecule studies have emerged over the last decade in particular, which have illuminated our knowledge of OXPHOS, most especially on model bacterial systems. Here, we discuss these recent findings of bacterial OXPHOS, many of which generate time-resolved information of the OXPHOS machinery with the native physiological context intact. These new investigations are transforming our knowledge of not only the molecular arrangement of OXPHOS components in live bacteria, but also of the way components dynamically interact with each other in a functional state. These new discoveries have important implications towards putative supercomplex formation in bacterial OXPHOS in particular.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2015 Published by Elsevier B.V. This is an author produced version of a paper accepted for publication in Biochimica et Biophysica Acta (BBA) - Bioenergetics. Uploaded in accordance with the publisher's self-archiving policy. |
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: | 16 Nov 2015 09:48 |
Last Modified: | 16 Oct 2024 12:41 |
Published Version: | https://doi.org/10.1016/j.bbabio.2015.10.008 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.bbabio.2015.10.008 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:91070 |
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