RESUMO
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 293â 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 2.25â Å and belonged to space group P21, with unit-cell parameters a = 97.3, b = 81.6, c = 116.2â Å, α = γ = 90, ß = 100.1°. The VM value is 2.85â Å(3)â Da(-1), indicating a solvent content of 56.8%.
Assuntos
Proteínas de Bactérias/química , Dioxigenases/química , Pseudomonas/enzimologia , Domínio Catalítico , Cristalização , Cristalografia por Raios X , Ferredoxinas/química , OxirreduçãoRESUMO
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 293â 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 1.74â Å and belonged to space group P6(5), with unit-cell parameters a = b = 92.0, c = 243.6â Å. The asymmetric unit contained a trimer of terminal oxygenase molecules.