Crystallization 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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1284-7. doi: 10.1107/S1744309113026754. Epub 2013 Oct 30.

Abstract

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 P6(5), with unit-cell parameters a = b = 92.0, c = 243.6 Å. The asymmetric unit contained a trimer of terminal oxygenase molecules.

Keywords: Janthinobacterium sp. J3; Rieske nonhaem iron oxygenase; carbazole 1,9a-dioxygenase; reduced form; terminal oxygenase component.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallization
  • Dioxygenases / chemistry*
  • Electron Transport Complex III / chemistry*
  • Enzyme Stability
  • Iron / metabolism*
  • Oxidation-Reduction
  • Proteobacteria / enzymology*
  • Spectrum Analysis
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Rieske iron-sulfur protein
  • Iron
  • Dioxygenases
  • carbazole 1,9a-dioxygenase
  • Electron Transport Complex III