Abstract
Isoelectrofocusing has been used to separate various chlorophyll-protein complexes of photosystem two (PS II). Light-harvesting complexes containing chlorophyll a and chlorophyll b (LHC II) were located in bands having p/s in the region of 4.5. At slightly higher pH other light-harvesting complexes containing little or no chlorophyll b were found. In the most basic region of the isoelectrofocusing gel, were located PS II core complexes characterized by containing the proteins of CP47, CP43, D 1, D 2 and α-subunit of cytochrome b559. The number of PS II core bands depended on the particular conditions employed for the separation procedure and in some cases were contaminated by CP 29. It is suggested that this heterogeneity resulting from different protonation states of the PS II.
The least-acidic PS II core complex (pI 5.5) was found to bind the herbicides atrazine, diuron and dinoseb. In contrast, a PS II core complex with a p / of 4.9 bound only diuron. Its inability to bind atrazine was shown to be due to the low pH but no such explanation could be found for dinoseb.
When atrazine-resistant mutant Senecio vulgaris was used, no binding of radioactive atra zine was observed with the PS II cores having a p i of 5.5. It is therefore suggested that the normal atrazine binding observed with PS II cores involves the high affinity site detected with intact membranes. With the PS II cores, however, this site has a reduced affinity probably due to structural modification in the D 1-polypeptide resulting from the isolation procedures.
Functional and mutational analysis of the light-harvesting chlorophyll a/b protein of thylakoid membranes.