Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17

Miyoun Yoo, Dockyu Kim, Gerben J. Zylstra, Beom Sik Kang, Eungbin KIm

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Hydroxylation of the non-growth substrate biphenyl by recombinant o-xylene dioxygenases from Rhodococcus sp. strain DK17 was studied through bioconversion experiments. The metabolites from the biphenyl hydroxylation by each enzyme were identified and quantified by gas chromatography-mass spectrometry. The L266F mutant enzyme produced much more 2-hydroxybiphenyl (2.43 vs. 0.1 μg/L) and 3-hydroxybiphenyl (1.97 vs. 0.03 μg/L) than the wild-type. Site-directed mutagenesis combined with structural and functional analyses indicated that hydrophobic interactions and shielding effects against water are important factors in the hydroxylation of biphenyl by the o-xylene dioxygenase. The residue at position 266 plays a key role in coordinating the reaction.

Original languageEnglish
Pages (from-to)724-728
Number of pages5
JournalResearch in Microbiology
Volume162
Issue number7
DOIs
Publication statusPublished - 2011 Sep 1

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Hydroxylation
Dioxygenases
Enzymes
Site-Directed Mutagenesis
Hydrophobic and Hydrophilic Interactions
Gas Chromatography-Mass Spectrometry
Water
diphenyl
Rhodococcus o-xylene dioxygenase

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Yoo, Miyoun ; Kim, Dockyu ; Zylstra, Gerben J. ; Kang, Beom Sik ; KIm, Eungbin. / Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17. In: Research in Microbiology. 2011 ; Vol. 162, No. 7. pp. 724-728.
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Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17. / Yoo, Miyoun; Kim, Dockyu; Zylstra, Gerben J.; Kang, Beom Sik; KIm, Eungbin.

In: Research in Microbiology, Vol. 162, No. 7, 01.09.2011, p. 724-728.

Research output: Contribution to journalArticle

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AB - Hydroxylation of the non-growth substrate biphenyl by recombinant o-xylene dioxygenases from Rhodococcus sp. strain DK17 was studied through bioconversion experiments. The metabolites from the biphenyl hydroxylation by each enzyme were identified and quantified by gas chromatography-mass spectrometry. The L266F mutant enzyme produced much more 2-hydroxybiphenyl (2.43 vs. 0.1 μg/L) and 3-hydroxybiphenyl (1.97 vs. 0.03 μg/L) than the wild-type. Site-directed mutagenesis combined with structural and functional analyses indicated that hydrophobic interactions and shielding effects against water are important factors in the hydroxylation of biphenyl by the o-xylene dioxygenase. The residue at position 266 plays a key role in coordinating the reaction.

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