Abstract
In this study, examination was made of chlorophyll (Chl) forms and energy transfer pathways in light-harvesting Chl a b - protein complex (LHC II) isolated from the siphonous green alga, Bryopsis maxima. Three major Chl a forms (Ca664, Ca672 and Ca679) and one minor form (Ca688) were resolved at 15°;C. Two Chl b forms were resolved at 648 and 653 nm. Based on the number of Chl bound to an apoprotein, two Chls a were assigned to each of the three major Chl a forms, and three and five Chls b, to Cb648 and Cb653, respectively. At 15°C, fluorescence spectra were identical, irrespective of the excitation conditions of Chl a, Chl b and siphonaxanthin. Fluorescence from Chl b was detected in addition to that from all Chl a forms. Very efficient energy transfer from siphonaxanthin or Chl b to Chl a and even uphill transfer from Chl a to Chl b, were noted by measurement of the excitation spectra. At 15°;C, the equilibrium of energy distribution was established among pigments. However, Chl b was found not to mediate energy transfer from siphonaxanthin to Chl a. The partial amino acid sequence of Bryopsis LHC II was similar to those of green algae and higher plants. The energy transfer pathway between pigments and molecular organization of Bryopsis LHC II were compared with LHC II isolated from spinach.
Published Version
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