Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments.

Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments.
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叶绿体 ATP 合酶的 c14 转子的结晶表明它含有色素。

DOI:
10.1016/j.bbabio.2008.05.009
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发表时间:
2008
期刊:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
Fromme,Petra
Fromme,Petra
中科院分区:
--
文献类型:
--
作者:
Varco-Merth,Benjamin;Fromme,Raimund;Wang,Meitian;Fromme,Petra

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ATP合成酶是地球上最重要的酶之一,因为它将质子的跨膜电化学势与ADP和无机磷合成ATP结合起来,为地球上几乎所有高等生命提供了主要的ATP来源。在三磷酸腺苷合成过程中,通常认为,在一个由10-15个c-亚基组成的寡聚环的每个蛋白质亚基上,一个保守的羧酸质子化是驱动转子部分(c10-14γɛ)相对于定子部分(α3β3δab2)旋转的。在这里,我们报道了从菠菜叶绿体酶中分离和结晶C亚基C14环的过程,衍射率高达2.8°。虽然之前并不知道三磷酸腺苷合成酶含有任何色素,但c-亚基的晶体具有强烈的黄色。色素分析表明,它们含有1个叶绿素和2个类胡萝卜素,从而首次表明叶绿体ATP合成酶含有辅因子,从而引发了色素在叶绿体ATP合成酶中的可能作用的问题。
The ATP synthase is one of the most important enzymes on earth as it couples the transmembrane electrochemical potential of protons to the synthesis of ATP from ADP and inorganic phosphate, providing the main ATP source of almost all higher life on earth. During ATP synthesis, stepwise protonation of a conserved carboxylate on each protein subunit of an oligomeric ring of 10–15 c-subunits is commonly thought to drive rotation of the rotor moiety (c10–14γɛ) relative to stator moiety (α3β3δab2). Here we report the isolation and crystallization of the c14-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 Å. Though ATP synthase was not previously known to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revealed that they contain 1 chlorophyll and 2 carotenoids, thereby showing for the first time that the chloroplast ATP synthase contains cofactors, leading to the question of the possible roles of the functions of the pigments in the chloroplast ATP synthase.
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