In vitro activity of C-20 methyltransferase, BchU, involved in bacteriochlorophyll c biosynthetic pathway in green sulfur bacteria
In vitro activity of C-20 methyltransferase, BchU, involved in bacteriochlorophyll c biosynthetic pathway in green sulfur bacteria
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DOI：
10.1016/j.febslet.2005.01.087
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发表时间：
2005-03-28
期刊：
影响因子：
3.5
通讯作者：
Tamiaki, H
中科院分区：
文献类型：
--
作者：
Harada, J;Saga, Y;Tamiaki, H
研究了细菌叶绿素c生物合成途径中二氢卟酚环C-20位甲基化的甲基转移酶BchU的活性。将来自光合绿色硫细菌Chlorobium tepidum的bchU基因在大肠杆菌中过表达为His标记的蛋白质（HiS（6）-BchU），并纯化该酶。在S-腺苷甲硫氨酸存在下，HiS 6-BchU在C-20位甲基化细菌脱镁叶绿酸锌d，得到细菌脱镁叶绿酸锌c。不含金属的bacteriopheophorbide d不能被BchU甲基化，这表明二氢卟酚中的中心金属应该被BchU识别。(c)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The activity of a methyltransferase, BchU, which catalyzes methylation at the C-20 position of chlorin ring in the biosynthetic pathway of bacteriochlorophyll c, was investigated in vitro. The bchU gene derived from the photosynthetic green sulfur bacterium, Chlorobium tepidum, was overexpressed in Escherichia coli as a His-tagged protein (HiS(6)-BchU), and the enzyme was purified. In the presence of S-adenosylmethionine, HiS6-BchU methylated zinc bacteriopheophorbide d at the C-20 position to give zinc bacteriopheophorbide c. Metal-free bacteriopheophorbide d could not be methylated by the BchU, indicating that the central metal in the chlorin should be required for the recognition by the BchU. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.