Single-molecule studies of the dynamics and interactions of bacterial OXPHOS complexes.
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 not only of 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. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, UK.
Tchern
T
Lenn
Biological Physics Sciences Institute (BPSI), Departments of Physics and Biology, University of York, York YO10 5DD, UK. Electronic address: mark.leake@york.ac.uk.
Mark C
MC
Leake
D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D045222:Electron Transport Chain Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D010085:Oxidative Phosphorylation
D001426:Bacterial Proteins; D045222:Electron Transport Chain Complex Proteins
E. coli; Fluorescent protein; Localization microscopy; Single particle tracking; Super-resolution; Supercomplexes