Dissecting the cytochrome c₂-reaction centre interaction in bacterial photosynthesis using single molecule force spectroscopy.

ABSTRACT: The reversible docking of small, diffusible redox proteins onto a membrane protein complex is a common feature of bacterial, mitochondrial and photosynthetic electron transfer (ET) chains. Spectroscopic studies of ensembles of such redox partners have been used to determine ET rates and dissociation constants. Here, we report a single-molecule analysis of the forces that stabilise transient ET complexes. We examined the interaction of two components of bacterial photosynthesis, cytochrome c₂ and the reaction centre (RC) complex, using dynamic force spectroscopy and PeakForce quantitative nanomechanical imaging. RC-LH1-PufX complexes, attached to silicon nitride AFM probes and maintained in a photo-oxidised state, were lowered onto a silicon oxide substrate bearing dispers

SUBMITTER: Vasilev C 

PROVIDER: S-EPMC6688529 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature