来自食芳烃诺卡氏菌IC177的咔唑1,9a-双加氧酶末端加氧酶组分的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of the terminal oxygenase component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177.
作者信息
Inoue Kengo, Ashikawa Yuji, Usami Yusuke, Noguchi Haruko, Fujimoto Zui, Yamane Hisakazu, Nojiri Hideaki
机构信息
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt 12):1212-4. doi: 10.1107/S1744309106044939. Epub 2006 Nov 4.
Abstract
Carbazole 1,9a-dioxygenase (CARDO) catalyzes the dihydroxylation of carbazole by angular-position (C9a) carbon bonding to the imino nitrogen and its adjacent C1 carbon. CARDO consists of a terminal oxygenase component and two electron-transfer components: ferredoxin and ferredoxin reductase. The terminal oxygenase component (43.9 kDa) of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177 was crystallized at 293 K using the hanging-drop vapour-diffusion method with PEG 8000 as the precipitant. The crystals diffract to 2.3 A resolution and belong to space group C2.
摘要
咔唑1,9a-双加氧酶（CARDO）通过角位（C9a）碳与亚氨基氮及其相邻的C1碳键合催化咔唑的二羟基化反应。CARDO由一个末端加氧酶组分和两个电子传递组分组成：铁氧化还原蛋白和铁氧化还原蛋白还原酶。来自嗜芳烃诺卡氏菌IC177的咔唑1,9a-双加氧酶的末端加氧酶组分（43.9 kDa）在293 K下采用悬滴气相扩散法，以聚乙二醇8000作为沉淀剂进行结晶。晶体的衍射分辨率为2.3 Å，属于空间群C2。
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