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Chromopeptides from Phytochrome and Phycocyanin. NM R Studies o f the Pfr and Pr Chromophore of Phytochrome and E,Z Isomeric Chromophores of Phycocyanin

Author:
Thümmler, Fritz, Rüdiger, Wolfhart, Cmiel, Edmund, Schneider, Siegfried
Source:
Zeitschrift für Naturforschung 2014 v.38 no.5-6 pp. 359-368
ISSN:
1865-7125
Subject:
Avena sativa, Spirulina maxima, amino acids, digestion, irradiation, isomers, nuclear magnetic resonance spectroscopy, pepsin, photochemistry, phycocyanin, phytochrome, seedlings
Abstract:
Chromopeptides were prepared by pepsin digestion of C-phycocyanin isolated from the cyano­bacterium Spirulina maxima and of phytochrome isolated from seedlings of Avena sativa L. The chromopeptides were characterized by amino acid analysis. The ZZZ configurated chromophore of the phycocyanin peptide was transformed into its ZZE configurated isomer by the method of Falk et al. (Mh. Chemie 111, 159- 175, 1980) which had previously been applied to biliverdins. The 500 MHz ¹HNMR spectrum of the ZZE configurated chromopeptides confirmed that its chromophore has the 15 E configuration. Irradiation yielded the ZZZ configurated isomer for which the ¹H NMR spectrum was also recorded. Native phytochrome was irradiated at 660 nm to yield the maximum amount of the Pfᵣ from (about 75% of total phytochrome). By digestion in the dark the previously described Pfᵣ chromopeptide was obtained. The 500 MHz ¹H NMR spectrum was compared with that of the ZZE phycocyanin peptide. It confirmed the 15 E con­figuration of the Pfᵣ chromopeptide. Irradiation yielded the 15 Z configurated Pᵣ chromopeptide. Comparison of the high resolution ¹HNMR spectra of Pfᵣ and Pᵣ chromopeptides revealed that not only the chromophore resonances but also those of some amino acids are changed by the Pfᵣ → Pᵣ chromopeptide phototransformation. The results are discussed in terms of chromophore amino acid interaction.
Agid:
5227038