Abstract
The chlorophyll (Chl) biosynthetic reactions were monitored during senescence of dark-incubated excised barley (Hordeum vulgare L. cv IB 65) leaves floated in double-distilled water or kinetin solution. Kinetin abolished the degradation of Chl but failed to check the net degradation of protochlorophyllide (Pchlide), suggesting that different sets of enzymes, i.e. kinetin sensitive and insensitive, are responsible for the degradation of Chl and Pchlide, respectively. Upon exposure of the leaves to light, the dark-accumulated Pchlide was efficiently phototransformed to chorophyllide (Chlide), even on the 7th d of dark incubation, demonstrating that the activity of Pchlide reductase, one of the late enzymes of the Chl biosynthetic pathway, is not substantially affected during senescence. The senescing leaves continued to synthesize Pchlide and Chlide until the 7th d, although at a reduced rate (20% of the 1st d). The decline of the rate of synthesis of Pchlide and Chlide is due to the loss of activity of two early enzymes of the Chl biosynthetic pathway, i.e. 5-aminolevulinic acid dehydratase and porphobilinogen deaminase. Kinetin substantially checked the loss of activity of these two enzymes.
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