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

Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1406-9. doi: 10.1107/S2053230X14018779. Epub 2014 Sep 25.

Abstract

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 Å(3) Da(-1), indicating a solvent content of 56.8%.

Keywords: Rieske nonhaem iron oxygenase; carbazole 1,9a-dioxygenase; electron-transfer complex; ferredoxin; terminal oxygenase.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Catalytic Domain
  • Crystallization
  • Crystallography, X-Ray
  • Dioxygenases / chemistry*
  • Ferredoxins / chemistry
  • Oxidation-Reduction
  • Pseudomonas / enzymology*

Substances

  • Bacterial Proteins
  • Ferredoxins
  • Dioxygenases
  • carbazole 1,9a-dioxygenase