BILIPROTEINS FROM THE BUTTERFLY Pieris brassicae STUDIED BY TIME-RESOLVED FLUORESCENCE AND COHERENT ANTI-STOKES RAMAN SPECTROSCOPY

The fluorescence decay time of the biliverdin IX7 chromophore present in biliproteins isolated from Pieris brassicae is determined to be 44 ± 3 ps. This value suggests a cyclic helical chromophore structure. The vibrational frequencies determined by CARS-spectroscopy are compared with those of model compounds. The data confirm that the chromophore in the protein-bound state adopts a cyclic-helical, flexible conformation

Bacteriochlorophyll aggregates in positively charged micelles

Micellar complexes were prepared from bacteriochlorophyll a and bacteriopheophytin a with the cationic detergents, cetyltrimethyl ammonium bromide and cetylpyridinium chloride. These complexes have spectroscopic properties (absorption, circular dichroism) which are very different from the ones formed with non-ionic detergents like Triton X-100, and also with anionic detergents. Bacteriochlorophyll a forms two complexes: One is blue-shifted and has excitonically coupled Qy transitions. The second one is extremely red-shifted. The unusual properties are suggested to result from interactions of the positively charged head-group of the detergent with the tetrapyrrole

RECONSTITUTION OF ALLOPHYCOCYANIN FROM Mastigocladus laminosus WITH ISOLATED LINKER POLYPEPTIDE

The core linker polypeptide Lc 8.9 was isolated from Mastigocladus laminosus and purified on a preparative scale. A method for the reconstitution of allophycocyanin (AP)—linker complexes from isolated polypeptides was developed. The complex (αAP(βAP)3 Lc 8.9 was reconstituted and compared to (αAPβAP) and (αAPβAP)3 by sucrose density gradient ultracentrifugation, absorption, fluorescence emission and circular dichroism spectroscopy. Differences in the spectra of reconstituted and of directly isolated AP complexes are discussed