Crystallization and preliminary X-ray diffraction studies of a novel ferredoxin involved in the dioxygenation of carbazole by Novosphingobium sp. KA1.
Novosphingobium sp. KA1 uses carbazole 1,9a-dioxygenase (CARDO) as the first dioxygenase in its carbazole-degradation pathway. The CARDO of KA1 contains a terminal oxygenase component and two electron-transfer components: ferredoxin and ferredoxin reductase. In contrast to the CARDO systems of other species, the ferredoxin component of KA1 is a putidaredoxin-type protein. This novel ferredoxin was crystallized at 293 K by the hanging-drop vapour-diffusion method using PEG MME 550 as the precipitant under anaerobic conditions. The crystals belong to space group C222(1) and diffraction data were collected to a resolution of 1.9 A (the diffraction limit was 1.6 A).
Umeda
Takashi
T
Biotechnology Research Center, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Katsuki
Junichi
J
Usami
Yusuke
Y
Inoue
Kengo
K
Noguchi
Haruko
H
Fujimoto
Zui
Z
Ashikawa
Yuji
Y
Yamane
Hisakazu
H
Nojiri
Hideaki
H
D002227:Carbazoles / Q000737:chemistry / Q000378:metabolism*; D003460:Crystallization; D005288:Ferredoxins / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism*; D042301:Sphingomonadaceae / Q000737:chemistry*; D014961:X-Ray Diffraction
D002227:Carbazoles; D005288:Ferredoxins; C041514:carbazole; D010100:Oxygen