Pigment structure and absorption properties of phycobilin chromophores

Pigment structure and absorption properties of phycobilin chromophores 

Properties of the major biliproteins from Mastigocladus laminosusFremyella diplosiphon and Chroomonas sp. = with known primary structure 

Protein - max A Quarternary structure Bilin content per subunit Bilin binding positions Number of residues % Homology between ap-subunits Refs. 

Peptide - linked PHYCOCYANOBILIN Peptide-linked PHYCOBILIVIOLIN 

Phycocyanin hexamers (a /3 )(, (A ax 620-635 nm), together with one of the linker polypeptides from the 30 kDa family, form the discs in the PBS rods attached to the APC core in the PBS [124,125], In several cyanobacteria the type of C-PC and the number of C-PC discs in the PBS rods is regulated by light intensity and/or light quality (chromatic adaptation, reviewed in Refs. 126 and 127). C-PC from M. laminosus (Fig. 12) has two PCB chromophores bound to the subunit, the second one being bound to Cys within an insertion of 10 amino acid residues at position 151-160 [113]. The PCB chromophores are singly bound to Cys and Cys - by ring A (Fig. 10). 

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