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Crystallization and preliminary X‐ray diffraction analyses of the redox‐controlled complex of terminal oxygenase and ferredoxin components in the Rieske nonhaem iron oxygenase carbazole 1,9a‐dioxygenase
Author(s) -
Matsuzawa Jun,
Aikawa Hiroki,
Umeda Takashi,
Ashikawa Yuji,
SuzukiMinakuchi Chiho,
Kawano Yoshiaki,
Fujimoto Zui,
Okada Kazunori,
Yamane Hisakazu,
Nojiri Hideaki
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14018779
Subject(s) - ferredoxin , oxygenase , dioxygenase , chemistry , crystallization , carbazole , oxidoreductase , heme oxygenase , crystallography , electron transport chain , electron transfer , redox , stereochemistry , photochemistry , inorganic chemistry , organic chemistry , heme , enzyme , biochemistry
The initial reaction in bacterial carbazole degradation is catalyzed by carbazole 1,9a‐dioxygenase, which consists of terminal oxygenase (Oxy), ferredoxin (Fd) and ferredoxin reductase components. The electron‐transfer complex between reduced Oxy and oxidized Fd was crystallized at 293 K using the hanging‐drop vapour‐diffusion method with PEG 3350 as the precipitant under anaerobic conditions. The crystal diffracted to a maximum resolution of 2.25 Å and belonged to space group P 2 1 , with unit‐cell parameters a = 97.3, b = 81.6, c = 116.2 Å, α = γ = 90, β = 100.1°. The V M value is 2.85 Å 3 Da −1 , indicating a solvent content of 56.8%.