Resonance Raman spectroscopy of a light-harvesting protein from the brown alga Laminaria saccharina.

Abstract

Resonance Raman spectroscopy of an antenna protein from the brown alga Laminaria saccharina has been used to investigate the molecular structure of this light-harvesting complex (LHC) at the level of its bound pigments, chlorophylls (chl) a and c and the xanthophyll fucoxanthin. Evidence has been obtained for the conservation of pigment structure during the isolation procedure used. Six chl a and two chl c molecules are indicated from the positions and relative contributions of stretching modes of their keto-carbonyl groups. Of special interest is the presence of a population of chls a having a protein-binding conformation highly similar to that seen in antenna proteins from higher plants, possibly indicating a common structural motif within this extended gene family. The eight fucoxanthin molecules evidenced are all in the all-trans conformation; however, one or two have a highly twisted configuration. The results are discussed in terms of common and varying structural features of LHCs in higher plants and algae.