The P700-chlorophyll a-protein of a blue-green alga

Abstract

The previously isolated chlorophyll a-protein of blue-green algae has been shown to contain P700 in a ratio of 1 reaction center molecule per 100 light-harvesting chlorophyll molecules. One-fifth of the molecules in the preparation contain P700 together with some 20 light-harvesting molecules, whereas the other molecules contain bulk chlorophyll only. Both pigment-protein entities are considered to be essentially the same and cannot be fractionated. An aggregate containing both types probably makes up the photochemical portion of the algal Photosystem I in vivo. The absorption and emission spectra of the pigment-protein are reported, as well as the spectral changes associated with the photochemical reaction. In addition to chlorophyll, carotenoid and protein the complex contains a quinone, which is not a plastoquinone. This unidentified quinone appears to participate in secondary electron transfer reactions occurring in the complex. Horse cytochrome c can be bound to the complex and will donate electrons to P +700 upon illumination. Current hypotheses for the identity of the primary electron acceptor were tested. It appears unlikely that flavins, pteridines or iron fill this role.