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Although significant insight has been gained into biochemical, genetic andstructural features of oxidative phosphorylation (OXPHOS) at the single-enzymelevel, relatively little was known of how the component complexes functiontogether in time and space until recently. Several pioneering single-moleculestudies have emerged over the last decade in particular, which have illuminatedour knowledge of OXPHOS, most especially on model bacterial systems. Here, wediscuss these recent findings of bacterial OXPHOS, many of which generatetime-resolved information of the OXPHOS machinery with the native physiologicalcontext intact. These new investigations are transforming our knowledge of notonly the molecular arrangement of OXPHOS components in live bacteria, but alsoof the way components dynamically interact with each other in a functionalstate. These new discoveries have important implications towards putativesupercomplex formation in bacterial OXPHOS in particular.

Single-molecule studies of the dynamics and interactions of bacterial OXPHOS complexes