483 



Atusi Takamiya, Hirosi Obata and Eijiro Yakushiji 



460 500 540 580 620 660 700 740 



Wovalenglh (mji) 



•■V - 



a^ 514- 



qI 



Q 



-1 0510 



CP668+ DP IP 



0320 



CP740+DPIPH2 





\ 

 CP., 



Q 

 0760 O 



0.74 



2 3 4 



Time(rnin) 



720 



Fig. 5 (left) Photoconversion of Chenopodium chlorophyll protein in presence 

 of mammalian cytochrome £ 



Fig. 6 (right) Photoconversion of Chenopodium chlorophyll protein 668 in 

 presence of DPIP 



hydrazin, EDTA, sodium borohydride, Pd with H2. and methyl viologen, the 

 first two named gave successful results with respect to the reversion of the 

 spectral changes in question. 



In an experiment shown in Fig. 1, the chlorophyll protein was first 

 photoconverted into the illuminated form, CP 743 , in the air (see above). After 

 the removal of oxygen, the cuvette was sealed and illuminated for 30 minutes 

 in the presence of added sodium hydrosulfite (10-3 m). About 97% of the 

 CP 743 previously formed was re-converted into the initial form, CP 668 . In 

 this case, the marked decreases in absorbancy at 458 m^ and 645 m/i caused 



400 



440 



480 



520 



720 



760 



560 600 640 680 



Wavelength (fn/j) 



Fig. 7 Photoreversion of Chenopodium chlorophyll protein in presence of 

 sodium hydrosulfite 



