Pramanik A M, Bingsmark S, Lindahl M, Baltscheffsky H, Baltscheffsky M, Andersson B
Department of Biochemistry, Arrhenius Laboratories, Stockholm University, Sweden.
Eur J Biochem. 1991 May 23;198(1):183-6. doi: 10.1111/j.1432-1033.1991.tb15999.x.
It has been shown for the first time that several photosystem-II thylakoid proteins and the main chlorophyll-a/b light-harvesting complex can be phosphorylated with inorganic pyrophosphate as phosphate donor. With pyrophosphate, as with ATP, the protein-kinase reaction is dependent on light or a strong reducing agent. The reaction which can be demonstrated in well-washed spinach thylakoids is dependent on electron transport and is controlled by the redox state of the plastoquinone pool. It is suggested that the pyrophosphate-dependent thylakoid protein phosphorylation is mediated by the same kinase which is responsible for the ATP-dependent protein phosphorylation. This pyrophosphate-dependent kinase activity may be derived from an evolutionary precursor from which ATP-dependent protein phosphorylation also developed.
首次表明,几种光系统II类囊体蛋白和主要的叶绿素a/b捕光复合体可以以无机焦磷酸作为磷供体进行磷酸化。对于焦磷酸,与ATP一样,蛋白激酶反应依赖于光或强还原剂。在充分洗涤的菠菜类囊体中可以证明的该反应依赖于电子传递,并受质体醌库的氧化还原状态控制。有人提出,依赖焦磷酸的类囊体蛋白磷酸化是由负责依赖ATP的蛋白磷酸化的同一种激酶介导的。这种依赖焦磷酸的激酶活性可能源自一种进化前体,依赖ATP的蛋白磷酸化也由此发展而来。