Abstract
Phytochrome is a plant photoreceptor involved in various photomorphogenic processes. The 124- kDa chromoprotein includes the linear methine- bridged tetrapyrrole phytochromobilin (POB) covalently bound to the polypeptide chain (Figure 1) [1]. Upon light absorption phytochrome can be converted from the physiologically inactive (Pr) to the active (Pfr) form. This reversible interconversion is most likely initiated by Z/E photoisomerization at one of the methine bridges of PФB followed by yet unknown conformational changes ot the chromophore and the protein environment. In the present work we have employed near-infrared Fourier-transform resonance Raman (RR) spectroscopy to study the photoinduced reaction cycle of recombinant phytochromes from oat (Phy A) and Synecchocystes sp. SPP 6803 (Syn_Phy) reconstituted with different chromophores, i. e., PФB and phycocyanobilin (PCB) in which the vinyl substituent of ring D is reduced (Figure 1).
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