The light harvesting complexes (LHC) of brown algae are embedded in plastid membranes. Besides chlorophyll a, these LHC bind chlorophyll c and fucoxanthin which are efficient for photosynthetic activity. The polypeptides are assembled in vivo into macromolecular complexes with molecular masses ranging from 120 to 700 kDa composed of two or several distinct components of 17-22 kDa. The chlorophyll c-fucoxanthin binding proteins are phylogenetically and structurally related to Chla/b-LHC protein. Indeed, the protein contains three membrane-spanning helices and possesses the conserved residues identified in green plants as stabilizing the tertiary structures or binding Chla molecules. However, the localization of Chlc and xanthophyll molecules is still unknown. Up to now, it is not clear if in the Chromophyta there are antennae transmitting the absorbed energy specifically to one or the other photosystems. The polypeptides are encoded by a nuclear multigene family but the total number of genes is not yet established in any species. Recently, the expression of Lhc genes has been shown to be regulated by light intensity and under the control of a blue receptor. As perspectives, the reconstitution of complexes in vitro could help to understand the binding of pigments to proteins. Cloning and characterization of the chlorophyll c fucoxanthin binding protein genes allow molecular biology approaches in the studies of the gene expression and also to develop a DNA transformation system for brown algae.