Phycobiliprotein-bilin linkage diversity. I. Structural studies on A- and D-ring-linked phycocyanobilins.
Phycocyanobilin (PCB) peptides alpha-1 PCB and beta-2T PCB were obtained by proteolytic degradation of Synechococcus 6301 C-phycocyanin. These peptides were found to have the following sequences. alpha-1 PCB Cys(PCB)-Ala-Arg beta-2T PCB Ile-Thr-Gln-Gly-Asp-Cys(PCB)-Ser-Ala. The peptides were examined by 1H NMR, circular dichroism spectroscopy, and secondary ion mass spectrometry. The 1H NMR data confirmed that in each case the bilin was attached through a single linkage, a thioether bond between the cysteinyl residue and the tetrapyrrole moiety. Comparison of the 1H NMR spectra of these peptides with those of appropriate model compounds showed that the thioether linkage in alpha-1 PCB was to the C-3' position and that in beta-2T PCB to the C-18' position on the bilin. Refluxing in neutral methanol under nitrogen led to the release of PCB from alpha-1 PCB but did not release the D-ring-linked tetrapyrrole from beta-2T. The above results together with those of an earlier study (Lagarias, J. C., Glazer, A. N., and Rapoport, H. (1979) J. Am. Chem. Soc. 101, 5030-5037) complete the determination of the mode of linkage of each of the three bilins on C-phycocyanin; two are linked through ring A and one through ring D. This is the first documented report of a singly D-ring-linked bilin.[1]References
- Phycobiliprotein-bilin linkage diversity. I. Structural studies on A- and D-ring-linked phycocyanobilins. Bishop, J.E., Lagarias, J.C., Nagy, J.O., Schoenleber, R.W., Rapoport, H., Klotz, A.V., Glazer, A.N. J. Biol. Chem. (1986) [Pubmed]
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