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

TL;DR

Recent single-molecule studies have advanced understanding of bacterial OXPHOS by revealing dynamic interactions and arrangements of complexes in live bacteria, with implications for supercomplex formation.

Contribution

This paper reviews recent single-molecule research on bacterial OXPHOS, highlighting new insights into the dynamics and organization of complexes in native conditions.

Findings

Time-resolved data on OXPHOS components in live bacteria

Evidence of dynamic interactions among OXPHOS complexes

Implications for supercomplex formation in bacteria

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.