Isolation of chlorophyll-protein complexes and quantification of electron transport components in Synura petersenil and Tribonema aequale.

The chlorophyll-protein complexes of the yellow alga Synura petersenii (Chrysophyceae) and the yellow-green alga Tribonema aequale (Xanthophyceae) were studied. The sodiumdodecylsulfate/sodiumdesoxycholate solubilized photosynthetic membranes of these species yielded three distinct pigment-protein complexes and a non-proteinous zone of free pigments, when subjected to SDS polyacrylamid gel electrophoresis. The slowest migrating protein was identical to complex I (CP I), the P-700 chlorophyll a-protein, which possessed 60 chlorophyll a molecules per reaction center in Tribonema and 108 in Synura. The zone of intermediate mobility contained chlorophyll a and carotenoids. The absorption spectrum of this complex was very similar to the chlorophyll a-protein of photosystem II (CP a), which is known from green plants. The fastest migrating pigment protein zone was identified as a light-harvesting chlorophyll-protein complex. In Synura this protein was characterized by the content of chlorophyll c and of fucoxanthin. Therefore this complex will be named as LH Chl a/c-fucocanthin protein. In addition to the separation of the chlorophyll-protein complexes the cellular contents of P-700, cytochrome f (bound cytochrome) and cytochrome c-553 (soluble cytochrome) were measured. The stoichiometry of cytochrome f: cytochrome c-553:P-700 was found to be 1:4:2.4 in Tribonema and 1:6:3.4 in Synurá.