CHLOROPLAST PROTEIN-PHOSPHORYLATION COUPLES PLASTOQUINONE REDOX STATE TO DISTRIBUTION OF EXCITATION-ENERGY BETWEEN PHOTOSYSTEMS
CHLOROPLAST PROTEIN-PHOSPHORYLATION COUPLES PLASTOQUINONE REDOX STATE TO DISTRIBUTION OF EXCITATION-ENERGY BETWEEN PHOTOSYSTEMS
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DOI：
10.1038/291025a0
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发表时间：
1981-01-01
期刊：
影响因子：
64.8
通讯作者：
ARNTZEN, CJ
中科院分区：
文献类型：
--
作者：
ALLEN, JF;BENNETT, J;ARNTZEN, CJ
在从豌豆叶分离的光合膜中，质体醌池的氧化还原状态控制叶绿体捕光色素蛋白复合物（LHC）的磷酸化水平和2个光系统之间吸收的激发能的分布。LHC多肽的磷酸化被认为是光合系统适应光波长变化的调节机制。通过测量32p从ATP到总膜蛋白的转移来测定分离的类囊体的蛋白激酶活性。
In photosynthetic membranes isolated from pea leaves, the redox state of the plastoquinone pool controls both the level of phosphorylation of the chloroplast light-harvesting pigment-protein complex (LHC) and distribution of absorbed excitation energy between the 2 photosystems. Phosphorylation of LHC polypeptides is proposed as the regulatory mechanism by which photosynthetic systems adapt to changing wavelengths of light. The protein kinase activity of isolated thylakoids was assayed measuring transfer of 32p from ATP to total membrane protein.