Harada Jiro, Saga Yoshitaka, Yaeda Yuki, Oh-Oka Hirozo, Tamiaki Hitoshi
Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.
FEBS Lett. 2005 Mar 28;579(9):1983-7. doi: 10.1016/j.febslet.2005.01.087.
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, His(6)-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.
在体外研究了一种甲基转移酶BchU的活性,该酶在细菌叶绿素c的生物合成途径中催化二氢卟吩环C-20位的甲基化反应。从光合绿硫细菌嗜热绿菌(Chlorobium tepidum)中获得的bchU基因在大肠杆菌中作为带His标签的蛋白(His(6)-BchU)进行过表达,并对该酶进行了纯化。在S-腺苷甲硫氨酸存在的情况下,His(6)-BchU使锌细菌脱镁叶绿素d在C-20位甲基化,生成锌细菌脱镁叶绿素c。无金属的细菌脱镁叶绿素d不能被BchU甲基化,这表明二氢卟吩中的中心金属是BchU识别所必需的。