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Res Microbiol. 2011 Sep;162(7):724-8. doi: 10.1016/j.resmic.2011.04.013. Epub 2011 Apr 30.

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

Author information

1
Department of Biology, Yonsei University, Seoul 120-749, South Korea.

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.

PMID:
21575716
DOI:
10.1016/j.resmic.2011.04.013
[Indexed for MEDLINE]

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