Characterization of an FMO variant of Chlorobaculum tepidum carrying bacteriochlorophyll a esterified by geranylgeraniol.

ABSTRACT: The Fenna-Matthews-Olson light-harvesting antenna (FMO) protein has been a model system for understanding pigment-protein interactions in the energy transfer process in photosynthesis. All previous studies have utilized wild-type FMO proteins from several species. Here we report the purification and characterization of the first FMO protein variant generated via replacement of the esterifying alcohol at the C-17 propionate residue of bacteriochlorophyll (BChl) a, phytol, with geranylgeraniol, which possesses three more double bonds. The FMO protein still assembles with the modified pigment, but both the whole cell absorption and the biochemical purification indicate that the mutant cells contain a much less mature FMO protein. The gene expression was checked using qRT-PCR, and none of the

SUBMITTER: Wen J 

PROVIDER: S-EPMC3954975 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature