Publication Details |
Category | Text Publication |
Reference Category | Journals |
DOI | 10.1111/j.1365-2958.2011.07856.x |
Title (Primary) | Enzymes involved in the anaerobic degradation of meta-substituted halobenzoates |
Author | Kuntze, K.; Kiefer, P.; Baumann, S.; Seifert, J.; von Bergen, M.; Vorholt, J.A.; Boll, M. |
Source Titel | Molecular Microbiology |
Year | 2011 |
Department | ISOBIO; METABOX; PROTEOM |
Volume | 82 |
Issue | 3 |
Page From | 758 |
Page To | 769 |
Language | englisch |
Abstract |
Organohalides are environmentally relevant compounds that can be degraded by aerobic and anaerobic microorganisms. The denitrifying Thauera chlorobenzoica is capable of degrading halobenzoates as sole carbon and energy source under anaerobic conditions. LC-MS/MS-based coenzyme A (CoA) thioester analysis revealed that 3-chloro- or 3-bromobenzoate were preferentially metabolized via non-halogenated CoA-ester intermediates of the benzoyl-CoA degradation pathway. In contrast, 3-fluorobenzoate, which does not support growth, was converted to dearomatized fluorinated CoA ester dead-end products. Extracts from cells grown on 3-chloro-/3-bromobenzoate catalysed the Ti(III)-citrate- and ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA was converted to a fluorinated cyclic dienoyl-CoA compound. The reductive dehalogenation reactions were identified as previously unknown activities of ATP-dependent class I benzoyl-CoA reductases (BCR) present in all facultatively anaerobic, aromatic compound degrading bacteria. A two-step dearomatization/H-halide elimination mechanism is proposed. A halobenzoate-specific carboxylic acid CoA ligase was characterized in T. chlorobenzoica; however, no such enzyme is present in Thauera aromatica, which cannot grow on halobenzoates. In conclusion, it appears that the presence of a halobenzoate-specific carboxylic acid CoA ligase rather than a specific reductive dehalogenase governs whether an aromatic compound degrading anaerobe is capable of metabolizing halobenzoates. |
Persistent UFZ Identifier | https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=11837 |
Kuntze, K., Kiefer, P., Baumann, S., Seifert, J., von Bergen, M., Vorholt, J.A., Boll, M. (2011): Enzymes involved in the anaerobic degradation of meta-substituted halobenzoates Mol. Microbiol. 82 (3), 758 - 769 10.1111/j.1365-2958.2011.07856.x |