Purification and characterization of NAD(P)H-dependent nitroreductase I from Klebsiella sp. C1 and enzymatic transformation of 2,4,6-trinitrotoluene

@article{Kim2005PurificationAC,
  title={Purification and characterization of NAD(P)H-dependent nitroreductase I from Klebsiella sp. C1 and enzymatic transformation of 2,4,6-trinitrotoluene},
  author={Hyoun-Young Kim and Hong-Gyu Song},
  journal={Applied Microbiology and Biotechnology},
  year={2005},
  volume={68},
  pages={766-773}
}
Three NAD(P)H-dependent nitroreductases that can transform 2,4,6-trinitrotoluene (TNT) by two reduction pathways were detected in Klebsiella sp. C1. Among these enzymes, the protein with the highest reduction activity of TNT (nitroreductase I) was purified to homogeneity using ion-exchange, hydrophobic interaction, and size exclusion chromatographies. Nitroreductase I has a molecular mass of 27 kDa as determined by SDS-PAGE, and exhibits a broad pH optimum between 5.5 and 6.5, with a… CONTINUE READING

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Flavin mononucleotide is most likely the natural flavin cofactor of this enzyme .
Flavin mononucleotide is most likely the natural flavin cofactor of this enzyme .
Unlike other nitroreductases , nitroreductase I was able to transform hydroxylaminodinitrotoluenes ( HADNT ) into aminodinitrotoluenes ( ADNT ) , and could reduce ortho isomers ( 2-HADNT and 2-ADNT ) more easily than their para isomers ( 4-HADNT and 4-ADNT ) .
Unlike other nitroreductases , nitroreductase I was able to transform hydroxylaminodinitrotoluenes ( HADNT ) into aminodinitrotoluenes ( ADNT ) , and could reduce ortho isomers ( 2-HADNT and 2-ADNT ) more easily than their para isomers ( 4-HADNT and 4-ADNT ) .
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