Horton P, Foyer C
Biochem J. 1983 Feb 15;210(2):517-21. doi: 10.1042/bj2100517.
Phosphorylation of the light-harvesting chlorophyll protein (LHCP) by the thylakoid protein kinase has been examined in the reconstituted chloroplast system. The level of phosphorylation by [32P]Pi was maximal at high light intensity and in the absence of 3-phosphoglycerate; dephosphorylation resulted from a subsequent decrease in light intensity or from the addition of 3-phosphoglycerate. Addition of ribose 5-phosphate, which acts as an ATP 'sink', also caused dephosphorylation. It is concluded that the degree of phosphorylation is dependent on the redox state and energy state of the system, thereby providing a mechanism for adapting light harvesting to the demands of carbon assimilation.
已在重建的叶绿体系统中研究了类囊体蛋白激酶对捕光叶绿素蛋白(LHCP)的磷酸化作用。在高光强度且不存在3-磷酸甘油酸的情况下,[32P]Pi的磷酸化水平最高;随后光强度降低或添加3-磷酸甘油酸会导致去磷酸化。添加作为ATP“汇”的5-磷酸核糖也会引起去磷酸化。得出的结论是,磷酸化程度取决于系统的氧化还原状态和能量状态,从而提供了一种使光捕获适应碳同化需求的机制。