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

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 P21, with unit-cell parameters a = 97.3, b = 81.6, c = 116.2 Å, α = γ = 90, β = 100.1°. The VM value is 2.85 Å3 Da−1, indicating a solvent content of 56.8%.

Source: Acta Crystallographica Section F - September 25, 2014 Category: Biochemistry Authors: Matsuzawa, J.Aikawa, H.Umeda, T.Ashikawa, Y.Suzuki-Minakuchi, C.Kawano, Y.Fujimoto, Z.Okada, K.Yamane, H.Nojiri, H. Tags: Rieske nonhaem iron oxygenase electron-transfer complex terminal oxygenase ferredoxin carbazole 1,9a-dioxygenase crystallization communications Source Type: research