Williams, R.E., Rathbone, D.A., Bruce, N.C. orcid.org/0000-0003-0398-2997 et al. (1 more author) (2004) Biotransformation of explosives by the old yellow enzyme family of flavoproteins. Applied and Environmental Microbiology. pp. 3566-3574. ISSN 0099-2240
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Copyright © 2004 American Society for Microbiology |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) > Centre for Novel Agricultural Products (CNAP) (York) |
Depositing User: | Sherpa Assistant |
Date Deposited: | 01 Apr 2005 |
Last Modified: | 22 Dec 2024 00:07 |
Published Version: | https://doi.org/10.1128/AEM.70.6.3566â¿¿3574.2004 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1128/AEM.70.6.3566â¿¿3574.2004 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:374 |