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2,4,6-Trinitrotoluene Reduction by Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum
Journal article   Open access   Peer reviewed

2,4,6-Trinitrotoluene Reduction by Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum

Shouqin Huang, Paul A. Lindahl, Chuanyue Wang, George N. Bennett, Frederick B. Rudolph, Joseph B. Hughes and Rice Univ., Houston, TX (US)
Applied and environmental microbiology, v 66(4), pp 1474-1478
01 Apr 2000
DOI: https://doi.org/10.1128/AEM.66.4.1474-1478.2000
PMID: 10742229
url
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC92010View
Published, Version of Record (VoR)Open Access (License Unspecified),  Open

Abstract

Enzymology and Protein Engineering
Purified CO dehydrogenase (CODH) from Clostridium thermoaceticum catalyzed the transformation of 2,4,6-trinitrotoluene (TNT). The intermediates and reduced products of TNT transformation were separated and appear to be identical to the compounds formed by C. acetobutylicum , namely, 2-hydroxylamino-4,6-dinitrotoluene (2HA46DNT), 4-hydroxylamino-2,6-dinitrotoluene (4HA26DNT), 2,4-dihydroxylamino-6-nitrotoluene (24DHANT), and the Bamberger rearrangement product of 2,4-dihydroxylamino-6-nitrotoluene. In the presence of saturating CO, CODH catalyzed the conversion of TNT to two monohydroxylamino derivatives (2HA46DNT and 4HA26DNT), with 4HA26DNT as the dominant isomer. These derivatives were then converted to 24DHANT, which slowly converted to the Bamberger rearrangement product. Apparent K m and k cat values of TNT reduction were 165 ± 43 μM for TNT and 400 ± 94 s −1 , respectively. Cyanide, an inhibitor for the CO/CO 2 oxidation/reduction activity of CODH, inhibited the TNT degradation activity of CODH.

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Biotechnology & Applied Microbiology
Microbiology
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