Biotransformation of explosives by the old yellow enzyme family of flavoproteins.
Several independent studies of bacterial degradation of nitrate ester explosives have demonstrated the involvement of flavin-dependent oxidoreductases related to the old yellow enzyme (OYE) of yeast. Some of these enzymes also transform the nitroaromatic explosive 2,4,6-trinitrotoluene (TNT). In this work, catalytic capabilities of five members of the OYE family were compared, with a view to correlating structure and function. The activity profiles of the five enzymes differed substantially; no one compound proved to be a good substrate for all five enzymes. TNT is reduced, albeit slowly, by all five enzymes. The nature of the transformation products differed, with three of the five enzymes yielding products indicative of reduction of the aromatic ring. Our findings suggest two distinct pathways of TNT transformation, with the initial reduction of TNT being the key point of difference between the enzymes. Characterization of an active site mutant of one of the enzymes suggests a structural basis for this difference.
Williams
Richard E
RE
Institute of Biotechnology, University of Cambridge, Cambridge CB2 1QT, United Kingdom.
Rathbone
Deborah A
DA
Scrutton
Nigel S
NS
Bruce
Neil C
NC
D001711:Biotransformation; D016972:Enterobacter cloacae / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D009252:NADPH Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014303:Trinitrotoluene / Q000378:metabolism*
D014303:Trinitrotoluene; D009252:NADPH Dehydrogenase