  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.
