Abstract
Azoreductases from Bacillus sp. B29 are NADH-dependent flavoenzymes which contain a flavin mononucleotide (FMN) as a prosthetic group and exist as homodimers composed of 23 kDa subunits. These enzymes catalyze the reductive degradation of various azo compounds by a ping-pong mechanism. In order to determine the structure-function relationship of the azo-dye reduction mechanism, an X-ray crystallographic study of azoreductases was performed. Selenomethionine-labelled AzrA (SeMet-AzrA) and AzrC were crystallized by the hanging-drop vapour-diffusion method. A crystal of SeMet-AzrA diffracted to 2.0 Å resolution and was determined to belong to space group P212121, with unit-cell parameters a = 56.9, b = 69.0, c = 105.4 Å. The native crystals of AzrC belonged to space group C2, with unit-cell parameters a = 192.0, b = 56.6, c = 105.5 Å, β = 115.7°, and diffracted to 2.21 Å resolution.
Original language | English |
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Pages (from-to) | 503-505 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 66 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2010 Apr 29 |
Externally published | Yes |
Keywords
- Azoreductases
- Bacillus sp. B29
- Flavoproteins
- NADH-dependent oxidoreductases
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics