X-ray structures of the peridinin-chlorophyll-protein reconstituted with different chlorophylls.
The peridinin-chlorophyll a-protein (PCP) from dinoflagellates is a soluble light harvesting antenna which gathers incoming photons mainly by the carotenoid peridinin. In PCPs reconstituted with different chlorophylls, the peridinin to chlorophyll energy transfer rates are well predicted by a Förster-like theory, but only if the pigment arrangements are identical in all PCPs. We have determined the X-ray structures of PCPs reconstituted with Chlorophyll-b (Chl-b), Chlorophyll-d (Chl-d) and Bacteriochlorophyll-a (BChl-a) to resolutions<or=2A. In all three cases the pigment arrangements are essentially the same as in native PCP. Hydrogen bonding is not responsible for preferential incorporation of "non-native" chlorophylls over Chl-a.
Schulte
Tim
T
Biophysics, Department of Biology and Biotechnology, Ruhr-University Bochum, D-44780 Bochum, Germany.
Hiller
Roger G
RG
Hofmann
Eckhard
E
D002338:Carotenoids / Q000737:chemistry* / Q000378:metabolism*; D002734:Chlorophyll / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray / Q000379:methods*; D015394:Molecular Structure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism*
D015800:Protozoan Proteins; C073227:peridinin chlorophyll-a protein, Dinophyceae; D002734:Chlorophyll; D002338:Carotenoids; C037184:chlorophyll b; C107509:chlorophyll d