Nitroreductase II Involved in 2,4,6-Trinitrotoluene Degradation: Purification and Characterization from Klebsiella sp. C1

Jung-Hye Shin; Hong-Gyu Song

doi:10.1007/s12275-008-0171-6

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Nitroreductase II Involved in 2,4,6-Trinitrotoluene Degradation: Purification and Characterization from Klebsiella sp. C1: Jung-Hye Shin , Hong-Gyu Song; Journal of Microbiology 2009;47(5):536-541.
DOI: https://doi.org/10.1007/s12275-008-0171-6
Published online: October 24, 2009

Division of Life Sciences, Kangwon National University, Chuncheon 200-701, Republic of Korea

Corresponding author: Hong-Gyu Song , Tel: 82-33-250-8545,

Received: 9 July 2008 • Accepted: 18 May 2009

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Abstract

Three 2,4,6-trinitrotoluene (TNT) nitroreductases from Klebsiella sp. C1 have different reduction capabilities that can degrade TNT by simultaneous utilization of two initial reduction pathways. Of these, nitroreductase II was purified to homogeneity by sequential chromatographies. Nitroreductase II is an oxygen- insensitive enzyme and reduces both TNT and nitroblue tetrazolium. The N-terminal amino acid sequence of the enzyme did not show any sequence similarity with those of other nitroreductases reported. However, it transformed TNT by the reduction of nitro groups like nitroreductase I. It had a higher substrate affinity and specific activity for TNT reduction than other nitroreductases, and it showed a higher oxidation rate of NADPH with the ortho-substituted isomers of TNT metabolites (2-hydroxylaminodinitrotoluene and 2-aminodinitrotoluene) than with para-substituted compounds (4-hydroxylaminodinitrotoluene and 4-aminodinitrotoluene).

Keywords: nitroreductase;Klebsiella sp.;enzyme purification;trinitrotoluene

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Nitroreductase II Involved in 2,4,6-Trinitrotoluene Degradation: Purification and Characterization from Klebsiella sp. C1

J. Microbiol. 2009;47(5):536-541. Published online October 24, 2009

DOI: https://doi.org/10.1007/s12275-008-0171-6

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