During oxygenic photosynthesis in cyanobacteria and chloroplasts of plants
and eukaryotic algae, conversion of light energy to biologically useful che
mical energy occurs in the specialized thylakoid membranes. Light-induced c
harge separation at the reaction centers of photosystems I and II, two mult
isubunit pigment-protein complexes in the thylakoid membranes, energeticall
y drive sequential photosynthetic electron transfer reactions in this membr
ane system. In general, in the prokaryotic cyanobacterial cells, the thylak
oid membrane is distinctly different from the plasma membrane. We have rece
ntly developed a two-dimensional separation procedure to purify thylakoid a
nd plasma membranes from the genetically widely studied cyanobacterium Syne
chocystis sp. PCC 6803. Immunoblotting analysis demonstrated that the purif
ied plasma membrane contained a number of protein components closely associ
ated with the reaction centers of both photosystems. Moreover,these protein
s were assembled in the plasma membrane as chlorophyll-containing multiprot
ein complexes, as evidenced from nondenaturing green gel and low-temperatur
e fluorescence spectroscopy data. Furthermore, electron paramagnetic resona
nce spectroscopic analysis showed that in the partially assembled photosyst
em I core complex in the plasma membrane, the P700 reaction center was capa
ble of undergoing light-induced charge separation. Based on these data, we
propose that the plasma membrane, and not the thylakoid membrane, is the si
te for a number of the early steps of biogenesis of the photosynthetic reac
tion center complexes in these cyanobacterial cells.