ABSTRACT
The bilin organization of three cryptomonad biliproteins (phycocyanins 612 and 645 and phycoerythrin 545) was examined in detail. Two others (phycocyanin 630 and phycoerythrin 566) were studied less extensively. Phycocyanin 645 and phycoerythrin 545 were suggested to have one bilin in each monomeric (alphabeta) unit of the dimer (alpha2beta2) isolated from the others, and the remaining six bilins may be in pairs. One pair was found across the monomer-monomer interface of the protein dimer, and two identical pairs were proposed to be within the monomer protein units. For phycocyanin 612, a major surprise was that a pair of bilins was apparently not found across the monomer-monomer interface, but the remaining bilins were distributed as in the other two cryptomonad proteins. The effect of temperature on the CD spectra of phycocyainin 612 demonstrated that two of the bands (one positive and one negative) behaved identically, which is required if they are coupled. The two lowest-energy CD bands of phycocyanin 612 originated from paired bilins, and the two higher-energy bands were from more isolated bilins. The paired bilins within the protein monomers contained the lowest-energy transition for these biliproteins. Using the bilins as naturally occurring reporter groups, phycocyanin 612 was shown to undergo a reversible change in tertiary structure at 40 degrees C. Protein monomers were shown to be functioning biliproteins. A hypothesis is that the coupled pair of bilins within the monomeric units offers important advantages for efficient energy migration, and other bilins transfer energy to this pair, extending the wavelength range or efficiency of light absorption.
