Open AccessCrystallization and preliminary X‐ray diffraction studies of the reduced form of the terminal oxygenase component of the Rieske nonhaem iron oxygenase system carbazole 1,9a‐dioxygenase
Author(s) -
Matsuzawa Jun,
Umeda Takashi,
Aikawa Hiroki,
Suzuki Chiho,
Fujimoto Zui,
Okada Kazunori,
Yamane Hisakazu,
Nojiri Hideaki
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113026754
Subject(s) - oxygenase , heme oxygenase , chemistry , crystallization , carbazole , terminal (telecommunication) , dioxygenase , component (thermodynamics) , crystallography , stereochemistry , photochemistry , physics , biochemistry , enzyme , organic chemistry , engineering , heme , telecommunications , thermodynamics
The initial reaction of bacterial carbazole degradation is catalysed by carbazole 1,9a‐dioxygenase, which consists of terminal oxygenase, ferredoxin and ferredoxin reductase components. The reduced form of the terminal oxygenase component was crystallized at 293 K by the hanging‐drop vapour‐diffusion method using PEG MME 550 as the precipitant under anaerobic conditions. The crystals diffracted to a resolution of 1.74 Å and belonged to space group P 6 5 , with unit‐cell parameters a = b = 92.0, c = 243.6 Å. The asymmetric unit contained a trimer of terminal oxygenase molecules.