Probing structure-function relationships in early events in photosynthesis using a chimeric photocomplex.

ABSTRACT: The native core light-harvesting complex (LH1) from the thermophilic purple phototrophic bacterium Thermochromatium tepidum requires Ca²⁺ for its thermal stability and characteristic absorption maximum at 915 nm. To explore the role of specific amino acid residues of the LH1 polypeptides in Ca-binding behavior, we constructed a genetic system for heterologously expressing the Tch. tepidum LH1 complex in an engineered Rhodobacter sphaeroides mutant strain. This system contained a chimeric pufBALM gene cluster (pufBA from Tch. tepidum and pufLM from Rba. sphaeroides) and was subsequently deployed for introducing site-directed mutations on the LH1 polypeptides. All mutant strains were capable of phototrophic (anoxic/light) gro

SUBMITTER: Nagashima KVP 

PROVIDER: S-EPMC5642683 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature