Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization

Dae-Young Kwon; Yanasinee Suma; Manish Kumar  Tiwari; Jeongyoon Choi; Lin-Woo Kang; Jung-Kul Lee; Han S. Kim

doi:10.1016/j.ibiod.2014.03.002

Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization

Dae-Young Kwon, Yanasinee Suma, Manish Kumar Tiwari, Jeongyoon Choi, Lin-Woo Kang, Jung-Kul Lee, Han S. Kim

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

This study was carried out to characterize hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 (Ar 1,2-HQD). The cphA-I gene encoding Ar 1,2-HQD was cloned and the enzyme was overexpressed for subsequent purification of the recombinant protein by Ni2þ-NTA affinity chromatography and fast protein liquid chromatography (FPLC). Purification of the enzyme by Ni2þ-NTA affinity
chromatography increased the substrate activity for various aromatic hydrocarbon intermediates by 9.4- to 12.9-fold. Subsequent purification of the enzyme by FPLC increased the activity by 51.7- to 65.2-fold. The substrate specificity of Ar 1,2-HQD indicated that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD). The deduced 304 amino acid sequence analysis
also revealed that Ar 1,2-HQD is an intradiol dioxygenase and it is related closely to 1,2-CTD. Its structure consisted of 5 a-helices in the N-terminal domain and 13 b-sheets in the C-terminal domain. The ferric ion was coordinated to two histidine residues and two tyrosine residues. The results of this study suggest that the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic
hydrocarbon contaminants.

Original language	English
Journal	International Biodeterioration & Biodegradation
ISSN	0964-8305
DOIs	https://doi.org/10.1016/j.ibiod.2014.03.002
Publication status	E-pub ahead of print - 2014
Externally published	Yes

Keywords

Arthrobacter chlorophenolicus A6
Aromatic hydrocarbon intermediates
Enzyme purification
Hydroxyquinol 1,2-dioxygenase
Structure characterization

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Kwon, D.-Y., Suma, Y., Tiwari, M. K., Choi, J., Kang, L.-W., Lee, J.-K., & Kim, H. S. (2014). Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization. International Biodeterioration & Biodegradation. Advance online publication. https://doi.org/10.1016/j.ibiod.2014.03.002

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title = "Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization",

abstract = "This study was carried out to characterize hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 (Ar 1,2-HQD). The cphA-I gene encoding Ar 1,2-HQD was cloned and the enzyme was overexpressed for subsequent purification of the recombinant protein by Ni2{\th}-NTA affinity chromatography and fast protein liquid chromatography (FPLC). Purification of the enzyme by Ni2{\th}-NTA affinity chromatography increased the substrate activity for various aromatic hydrocarbon intermediates by 9.4- to 12.9-fold. Subsequent purification of the enzyme by FPLC increased the activity by 51.7- to 65.2-fold. The substrate specificity of Ar 1,2-HQD indicated that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD). The deduced 304 amino acid sequence analysis also revealed that Ar 1,2-HQD is an intradiol dioxygenase and it is related closely to 1,2-CTD. Its structure consisted of 5 a-helices in the N-terminal domain and 13 b-sheets in the C-terminal domain. The ferric ion was coordinated to two histidine residues and two tyrosine residues. The results of this study suggest that the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic hydrocarbon contaminants.",

keywords = "Arthrobacter chlorophenolicus A6, Aromatic hydrocarbon intermediates, Enzyme purification, Hydroxyquinol 1,2-dioxygenase, Structure characterization",

author = "Dae-Young Kwon and Yanasinee Suma and Tiwari, {Manish Kumar} and Jeongyoon Choi and Lin-Woo Kang and Jung-Kul Lee and Kim, {Han S.}",

year = "2014",

doi = "10.1016/j.ibiod.2014.03.002",

language = "English",

journal = "International Biodeterioration & Biodegradation",

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Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization. / Kwon, Dae-Young; Suma, Yanasinee; Tiwari, Manish Kumar et al.
In: International Biodeterioration & Biodegradation, 2014.

Research output: Contribution to journal › Journal article › Research › peer-review

TY - JOUR

T1 - Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization

AU - Kwon, Dae-Young

AU - Suma, Yanasinee

AU - Tiwari, Manish Kumar

AU - Choi, Jeongyoon

AU - Kang, Lin-Woo

AU - Lee, Jung-Kul

AU - Kim, Han S.

PY - 2014

Y1 - 2014

N2 - This study was carried out to characterize hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 (Ar 1,2-HQD). The cphA-I gene encoding Ar 1,2-HQD was cloned and the enzyme was overexpressed for subsequent purification of the recombinant protein by Ni2þ-NTA affinity chromatography and fast protein liquid chromatography (FPLC). Purification of the enzyme by Ni2þ-NTA affinity chromatography increased the substrate activity for various aromatic hydrocarbon intermediates by 9.4- to 12.9-fold. Subsequent purification of the enzyme by FPLC increased the activity by 51.7- to 65.2-fold. The substrate specificity of Ar 1,2-HQD indicated that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD). The deduced 304 amino acid sequence analysis also revealed that Ar 1,2-HQD is an intradiol dioxygenase and it is related closely to 1,2-CTD. Its structure consisted of 5 a-helices in the N-terminal domain and 13 b-sheets in the C-terminal domain. The ferric ion was coordinated to two histidine residues and two tyrosine residues. The results of this study suggest that the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic hydrocarbon contaminants.

AB - This study was carried out to characterize hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 (Ar 1,2-HQD). The cphA-I gene encoding Ar 1,2-HQD was cloned and the enzyme was overexpressed for subsequent purification of the recombinant protein by Ni2þ-NTA affinity chromatography and fast protein liquid chromatography (FPLC). Purification of the enzyme by Ni2þ-NTA affinity chromatography increased the substrate activity for various aromatic hydrocarbon intermediates by 9.4- to 12.9-fold. Subsequent purification of the enzyme by FPLC increased the activity by 51.7- to 65.2-fold. The substrate specificity of Ar 1,2-HQD indicated that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD). The deduced 304 amino acid sequence analysis also revealed that Ar 1,2-HQD is an intradiol dioxygenase and it is related closely to 1,2-CTD. Its structure consisted of 5 a-helices in the N-terminal domain and 13 b-sheets in the C-terminal domain. The ferric ion was coordinated to two histidine residues and two tyrosine residues. The results of this study suggest that the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic hydrocarbon contaminants.

KW - Arthrobacter chlorophenolicus A6

KW - Aromatic hydrocarbon intermediates

KW - Enzyme purification

KW - Hydroxyquinol 1,2-dioxygenase

KW - Structure characterization

U2 - 10.1016/j.ibiod.2014.03.002

DO - 10.1016/j.ibiod.2014.03.002

M3 - Journal article

SN - 0964-8305

JO - International Biodeterioration & Biodegradation

JF - International Biodeterioration & Biodegradation

ER -

Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization

Abstract

Keywords

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