Abstract
Abstract Thylakoid protein phosphorylation was assayed in vitro with isolated thylakoids of Scenedesmus obliquus by irradiation with monochromatic light of different wavelengths and equal photon fluences. The action spectrum for light‐activated protein phosphorylation showed two maxima at 450 and 679 nm. A minimum of activity was reached around 580 nm. At this wavelength, the level of protein phosphorylation barely differed from that of dark‐incubated samples. The action spectrum of thylakoid protein phosphorylation resembled the chlorophyll absorption spectrum obtained in vivo. The results show that chlorophyll is the photoreceptor for thylakoid membrane phosphorylation.
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