Biotransformation of explosives by the old yellow enzyme family of flavoproteins

R.E. Williams; D.A. Rathbone; N.C. Bruce; N.S. Scrutton

doi:10.1128/AEM.70.6.3566â¿¿3574.2004

Biotransformation of explosives by the old yellow enzyme family of flavoproteins

R.E. Williams, D.A. Rathbone, N.C. Bruce, N.S. Scrutton

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Abstract

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.

Original language	English
Pages (from-to)	3566-3574
Number of pages	8
Journal	Applied and Environmental Microbiology
Volume	70
Issue number	6
DOIs	https://doi.org/10.1128/AEM.70.6.3566â¿¿3574.2004
Publication status	Published - 2004

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title = "Biotransformation of explosives by the old yellow enzyme family of flavoproteins",

abstract = "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.",

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T1 - Biotransformation of explosives by the old yellow enzyme family of flavoproteins

AU - Williams, R.E.

AU - Rathbone, D.A.

AU - Bruce, N.C.

AU - Scrutton, N.S.

PY - 2004

Y1 - 2004

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AB - 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.

U2 - 10.1128/AEM.70.6.3566â¿¿3574.2004

DO - 10.1128/AEM.70.6.3566â¿¿3574.2004

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