Chromophore attachment in phycocyanin. Functional amino acids of phycocyanobilin--alpha-phycocyanin lyase and evidence for chromophore binding.

@article{Zhao2006ChromophoreAI,
  title={Chromophore attachment in phycocyanin. Functional amino acids of phycocyanobilin--alpha-phycocyanin lyase and evidence for chromophore binding.},
  author={Kai-Hong Zhao and Dong Wu and Ling Zhang and Ming Zhou and Stephan B{\"o}hm and Claudia Bubenzer and H. T. van der Scheer},
  journal={The FEBS journal},
  year={2006},
  volume={273 6},
  pages={1262-74}
}
Covalent attachment of phycocyanobilin (PCB) to the alpha-subunit of C-phycocyanin, CpcA, is catalysed by the heterodimeric PCB : CpcA lyase, CpcE/F [Fairchild CD, Zhao J, Zhou J, Colson SE, Bryant DA & Glazer AN (1992) Proc Natl Acad Sci USA89, 7017-7021]. CpcE and CpcF of the cyanobacterium, Mastigocladus laminosus PCC 7603, form a 1 : 1 complex. Lyase-mutants were constructed to probe functional domains. When in CpcE (276 residues) the N terminus was truncated beyond the R33YYAAWWL motif, or… CONTINUE READING