2,4,6-trinitrotoluene reduction by carbon monoxide dehydrogenase from Clostridium thermoaceticum

Article Abstract:

Researchers describe the bioremediation of 2,4,6-trinitrotoluene (TNT) by Clostridium thermoaceticum. TNT is a common soil contaminant on many Department of Defense facilities.

Bioremediation

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2,4,6-trinitrotoluene reduction by an Fe-only hydrogenase in Clostridium acetobutylicum

Article Abstract:

Results reveal that the primary catalyst Fe-only hydrogenase reduces 2,4,6-trinitrotoluene nitro substituents to their cognate hydroxylamines in whole-cell systems of Clostridium acetobutylicum. A mechanism for the reduction reaction is proposed.

United States, Enzymes, Other Basic Organic Chemical Manufacturing, Cyclic Crude and Intermediate Manufacturing, Explosives, Trinitrotoluene, Physiological aspects, Microbial metabolism, Biodegradation, TNT (Trinitrotoluene)

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Characterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1,2-propanediol

Article Abstract:

A gene encoding a putative 150-amino acid methylglyoxal synthase was detected in Clostridium acetobutylicum ATCC 824. The enzyme as overexpressed in Escherichia coli and purified. Methylglyoxal synthase was found to have a molecular mass of 60 kDa and an optimum pH of 7.5. The K(sub m) and V(sub max) values for the substrate dihydroxyacetone phosphate were 0.53 mM and 1.56 mmol/min/microgram, respectively. When E. coli glycerol dehydrogenase was coexpressed with methylglyoxal synthase in E. coli BL21, 3.9 mM 1,2-propanediol was generated.

Microbial enzymes

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