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

Authors
Lee, Jeong HyePark, Ae KyungOh, Jae SoonLee, Ki SeogChi, Young Min
Issue Date
8월-2013
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
NAO; nitro compounds; nitroalkane oxidase; Pseudomonas aeruginosa
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.69, pp.888 - 890
Indexed
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
69
Start Page
888
End Page
890
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/102537
DOI
10.1107/S1744309113017235
ISSN
2053-230X
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 1.9 angstrom and belonged to the primitive orthorhombic space group P2(1), with unit-cell parameters a = 70.06, b = 55.43, c = 87.74 angstrom, beta = 96.56 degrees for native NAO and a = 69.89, b = 54.83, c = 88.20 angstrom, beta = 95.79 degrees 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 2.48 angstrom(3) Da(-1), with estimated solvent contents of 46.50 and 50.37%, respectively.
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생명과학대학 (생명공학부)
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