DocumentCode
3346633
Title
Notice of Retraction
Cloning, Expression, and Characterization of Recombinant Hydroxyquinol-1, 2-Dioxygenase from Pseudomonas sp. strain HS-D38
Author
Xueting Yang ; Yongze Yuan ; Jian Liu ; Kimoto, C. ; Li Xiong ; Hui Geng ; Deli Liu ; Xianfang Wen ; Hailing Xi ; Yongliang Zheng
Author_Institution
Hubei Key Lab. of Genetic Regul. & Integrative Biol., Central China Normal Univ., Wuhan, China
fYear
2011
fDate
10-12 May 2011
Firstpage
1
Lastpage
4
Abstract
Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Hydroxyquinol 1, 2-Dioxygenase is a key enzyme for p-nitrophenol (PNP) catabolism in bacterium. In this paper, we cloned a pnpC gene encoding hydroxyquinol-1, 2-dioxygenase from Pseudomonas sp. strain HS-D38 that could degrade PNP efficiently. The open reading frame of the pnpC contained 873 nucleotides and the deduced molecular mass of gene product (PnpC) was 33 kDa The recombinant enzyme was highly expressed in E. coli BL21(DE3) as a histidine-tag fusion protein and purified to homogeneity by Ni-NAT affinity chromatography. The specific activity of the purified protein reached at 9.3 U/mg. The maximum activity of the recombinant enzyme towards catechol was exhibited at 45 V and pH5.0. The enzyme activity could be stimulated by 0.2 mM of Fe3+, Fe2+, Cu2+, Zn2+, Mn2+, and Co2+. The above results provided useful information for PnpC application in biodegradation of PNP pollutants.
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Hydroxyquinol 1, 2-Dioxygenase is a key enzyme for p-nitrophenol (PNP) catabolism in bacterium. In this paper, we cloned a pnpC gene encoding hydroxyquinol-1, 2-dioxygenase from Pseudomonas sp. strain HS-D38 that could degrade PNP efficiently. The open reading frame of the pnpC contained 873 nucleotides and the deduced molecular mass of gene product (PnpC) was 33 kDa The recombinant enzyme was highly expressed in E. coli BL21(DE3) as a histidine-tag fusion protein and purified to homogeneity by Ni-NAT affinity chromatography. The specific activity of the purified protein reached at 9.3 U/mg. The maximum activity of the recombinant enzyme towards catechol was exhibited at 45 V and pH5.0. The enzyme activity could be stimulated by 0.2 mM of Fe3+, Fe2+, Cu2+, Zn2+, Mn2+, and Co2+. The above results provided useful information for PnpC application in biodegradation of PNP pollutants.
Keywords
biochemistry; chromatography; cobalt; copper; enzymes; genetics; iron; manganese; microorganisms; molecular biophysics; molecular weight; pH; purification; zinc; Co; Cu; E. coli BL21; Fe; Mn; PNP pollutants; Pseudomonas sp. strain HS-D38; Zn; affinity chromatography; bacterium; biodegradation; catechol; enzyme expression; histidine-tag fusion protein; molecular mass; pH; pnpC gene; pnpC gene cloning; purification; recombinant hydroxyquinol-1, 2-dioxygenase; voltage 45 V; Cloning; Degradation; Microorganisms; Proteins; Strain; Temperature measurement;
fLanguage
English
Publisher
ieee
Conference_Titel
Bioinformatics and Biomedical Engineering, (iCBBE) 2011 5th International Conference on
Conference_Location
Wuhan
ISSN
2151-7614
Print_ISBN
978-1-4244-5088-6
Type
conf
DOI
10.1109/icbbe.2011.5781591
Filename
5781591
Link To Document