Abstract
Illumination of 3 day old etiolated radish seedlings with continuous white light results in a progressive accumulation of chlorophyll a and b. Both pigments are bound in a different way to the thylakoid chlorophyll-proteins, which appear parallel to the formation of chlorophylls. By applying the SDS-PAGE method to SDS-digested chloroplasts, it was possible to show that the chloroplasts of radish cotyledons contain the typical chlorophyll proteins LHCP1-3, CPa, CPI and CPIa which have been found in other plants. Between LHCP1 and CPI an additional chlorophyll protein is detected with the spectral properties of a LHCP; it is termed here LHCPy.
When the green plants are transferred to continuous darkness, chlorophylls and the chlorophyll-proteins are progressively degraded. At an early stage of greening chlorophyll b is destroyed at a much higher rate in darkness than chlorophyll a, which yields high chlorophyll a/b ratios. This is paralleled by a faster decrease in the level of the corresponding chlorophyll a/b-protein LHCP3 than of CPI. At a later stage of greening, after the end of the logarithmic chlorophyll accumulation, the chlorophylls a and b and also the LHCP3 and CPI are destroyed in continuous darkness at equal rates; the a/b ratios and the LHCP3/CPI ratios are then little different from the light control.
The data indicate that at an early stage of greening the light-harvesting chlorophyll a/b-protein LHCP3 is less stable than the other chlorophyll-proteins (CPI, CPIa, CPa), which contain pre dominantly chlorophyll a.
The ratio chlorophyll a to β-carotene (a/c ratio) of CPIa, CPI and CPa is about 10, while that of the LHCP1-3 is found to be between 150 to 300. We therefore propose using the a/c ratio to define the chlorophyll-proteins which, besides the absorption spectra, is the most suitable parameter.
Replacement of Histidines of Light Harvesting Chlorophyll a/b Binding Protein II Disrupts Chlorophyll-Protein Complex Assembly
