Energy transfer in the peridinin-chlorophyll protein complex reconstituted with mixed chlorophyll sites.

ABSTRACT: We use femtosecond transient absorption spectroscopy to study chlorophyll (Chl)-Chl energy transfer in the peridinin-chlorophyll protein (PCP) reconstituted with mixtures of either chlorophyll b (Chlb) and Chld or Chla and bacteriochlorophyll a (BChla). Analysis of absorption and transient absorption spectra demonstrated that reconstitution with chlorophyll mixtures produces a significant fraction of PCP complexes that contains a different Chl in each domain of the PCP monomer. The data also suggest that binding affinity of Chla is less than that of the other three Chl species. By exciting the Chl species lying at higher energy, we obtained energy transfer times of 40 +/- 5 ps (Chlb-Chld) and 59 +/- 3 ps (Chla-BChla). The experimental values match those obtained from the Förster equation,

SUBMITTER: Polivka T 

PROVIDER: S-EPMC2275708 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature