Arrangement of Chlorophyll Protein Complexes Determines Chloroplast Structure

Abstract

It is believed that there is a close relation between chloroplast structure and function. To support this statement we studied chloroplast structure and function in two plant species with a different susceptibility for chilling-bean (Phaseolus vulgaris)-CS (chilling sensitive) plant and pea (Pisum sativum)-CT (chilling tolerant) plant. The fluorescence difference spectrum bean-minus-pea indicated that there is relatively less core PSII and external antenna complexes associated with PSII and PSI in bean than in pea thylakoids. Instead the appearance of the emission band at around 705 nm suggested that the aggregated form of LHCII is more frequent in bean thylakoid membranes than in pea ones. Bigger appressed domains (grana) occurred in pea as compared to bean revealed by 3D structure of chloroplasts obtained using confocal laser scanning fluorescence micro-scopy CLSM).