Circular Dichroism and Other Optical Properties of Antenna Chlorophyll Proteins from Higher Plants

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Abstract
We report the measurement of the room‐temperature optical properties of antenna chlorophyll proteins (prepared with sodium dodecyl sulfate membrane solubilization) from six plant species of five different orders: pea (Pisum sativum), soy (Glycine max), barley (Hordeum vulgare), spinach (Spinacea oleracea), yew (Taxus canadensis), and fern (Onoclea sensibilis). All six species' antenna protein preparations exhibit optical spectra which are similar in great detail, implying similar internal chromophore arrangements from species to species. Features of the spectra thought due to chromophore interactions disappear upon heat denaturation. A model proposed by Van Metter for spinach chlorophyll protein has been revised and is consistent with all the data presented here.