Abstract
Cryptomonad biliproteins do not form higher aggregates like phycobili-somes (PBS) in cyanobacteria and red algae, but instead form heterotetra-mers (α1)β(α2)β (1,2). Phycocyanin-645 from Chroomonas sp. is built up of four subunits: two different α-subunits, α1 and α2 with a molecular weight of 9 kDa and 10 kDa, respectively, and two β-subunits of molecular weight 19 kDa (2,3,4). in the PC-645 molecule, which fulfills the same function as the much larger PBS, three different types of chromophores are located: two blue PCB-chromophores and one purple cryptoviolin chromophore are attached to the β-subunit and one green biliverdin-like chromophore on each of the different a-subunits (5). Amino-acid sequences of cryptomonad biliproteins and cyanobacterial C-phycoerythrin were determined both to obtain insight into structural, functional and phylogenetic relationships of these antenna proteins and to support the determination of the three-dimensional structure of PC-645 crystals (6).
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© 1987 Martinus Nijhoff Publishers, Dordrecht
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Sidler, W.A., Nutt, H., Kumpf, B., Zuber, H., Wehrmeyer, W., Brenzel, A. (1987). Structural Principles of Cryptomonad Biliproteins and Cyanobacterial Phycobiliproteins. In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-3535-8_37
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DOI: https://doi.org/10.1007/978-94-009-3535-8_37
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