A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin-dependent enzymes.

ABSTRACT: Halogenated phenol and nitrophenols are toxic compounds that are widely accumulated in the environment. Enzymes in the had operon from the bacterium Ralstonia pickettii DTP0602 have the potential for application as biocatalysts in the degradation of many of these toxic chemicals. HadA monooxygenase previously was identified as a two-component reduced FAD (FADH^-)-utilizing monooxygenase with dual activities of dehalogenation and denitration. However, the partner enzymes of HadA, that is, the flavin reductase and quinone reductase that provide the FADH^- for HadA and reduce quinone to hydroquinone, remain to be identified. In this report, we overexpressed and purified the flavin reductases, HadB and HadX, to investigate their functional and catalytic proper

SUBMITTER: Pimviriyakul P 

PROVIDER: S-EPMC6290146 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature