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Fourier transform near-infrared resonance Raman spectroscopic study of the α-subunit of phycoerythrocyanin and phycocyanin from the cyanobacterium Mastigocladus laminosus
Citation key ISI:000077127000011
Author Kneip, C and Parbel, A and Foerstendorf, H and Scheer, H and Siebert, F and Hildebrandt, P
Pages 939-944
Year 1998
ISSN 0377-0486
Address BAFFINS LANE CHICHESTER, W SUSSEX PO19 1UD, ENGLAND
Journal J. Raman Spec.
Volume 29
Number 10-11
Month OCT-NOV
Publisher JOHN WILEY & SONS LTD
Abstract The isolated alpha-subunits of the light-harvesting pigments phycoerythrocyanin (PEC) and C-phycocyanin (CPC) of Mastigocladus laminosus were studied by resonance Raman (RR) spectroscopy, The results for PEC indicate that the photoconversion of the tetrapyrrole chromophore from the Z,Z to the Z,E configuration is associated with structural changes which are largely restricted to the photoisomerization site, i.e. the methine-bridge C-D. Evidently the rotation around this double bond is not complete in the first intermediate which can be detected after the photochemical event. The subsequent decay to the stable Z,E isomer at T > -30 degrees C is associated with conformational relaxations of the remainder of the chromophore, Thus, the PEC photoconversion differs substantially from that of the plant photoreceptor phytochrome, which exhibits more extended changes of the chromophore structure and its interactions with the protein environment during the photoconversion. (C) 1998 John Wiley & Sons, Ltd.
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