Expression, purification and preliminary X-ray crystallographic analysis of nitroalkane oxidase (NAO) from Pseudomonas aeruginosa

Jeong Hye Lee, Ae Kyung Park, Jae Soon Oh, Ki Seog Lee, Young Min Chi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Nitroalkane oxidase (NAO) is a flavin-dependent enzyme which catalyses the oxidation of nitroalkanes to the corresponding aldehydes or ketones, nitrite and hydrogen peroxide. In order to better understand the structure and function of this enzyme, NAO from Pseudomonas aeruginosa was purified and crystallized as a native and a selenomethionine-substituted (SeMet) enzyme. Both crystals diffracted to a resolution of 1.9Å and belonged to the primitive orthorhombic space group P21, with unit-cell parameters a = 70.06, b = 55.43, c = 87.74Å, β = 96.56° for native NAO and a = 69.89, b = 54.83, c = 88.20Å, β = 95.79° for SeMet NAO. Assuming the presence of two molecules in the asymmetric unit in both crystals, the Matthews coefficients (V M) for native and SeMet NAO were calculated to be 2.30 and 2. 48Å3Da-1, with estimated solvent contents of 46.50 and 50.37%, respectively.

Original languageEnglish
Pages (from-to)888-890
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number8
DOIs
Publication statusPublished - 2013 Aug 1

Fingerprint

pseudomonas
oxidase
purification
Pseudomonas aeruginosa
Purification
Selenomethionine
X-Rays
X rays
enzymes
peroxides
x rays
Enzymes
Crystals
nitrites
Nitrites
Ketones
hydrogen peroxide
aldehydes
Aldehydes
ketones

Keywords

  • NAO
  • nitro compounds
  • nitroalkane oxidase
  • Pseudomonas aeruginosa

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

Expression, purification and preliminary X-ray crystallographic analysis of nitroalkane oxidase (NAO) from Pseudomonas aeruginosa. / Lee, Jeong Hye; Park, Ae Kyung; Oh, Jae Soon; Lee, Ki Seog; Chi, Young Min.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 8, 01.08.2013, p. 888-890.

Research output: Contribution to journalArticle

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