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ATP-dependent/-independent enzymatic ring reductions involved in the anaerobic catabolism of naphthalene

Lookup NU author(s): Emeritus Professor Bernard Golding


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Polycyclic aromatic hydrocarbons are among the most hazardous environmental pollutants. However, in contrast to aerobic degradation, the respective degradation pathways in anaerobes are greatly unknown which has so far prohibited many environmental investigations. In this work, we studied the enzymatic dearomatization reactions involved in the degradation of the PAH model compounds naphthalene and 2-methylnaphthalene in the sulfate-reducing enrichment culture N47. Cell extracts of N47 grown on naphthalene catalysed the sodium dithionite-dependent four-electron reduction of the key intermediate 2-naphthoyl-coenzyme A (NCoA) to 5,6,7,8-tetrahydro-2-naphthoyl-CoA (THNCoA). The NCoA reductase activity was independent of ATP and was, surprisingly, not sensitive to oxygen. In cell extracts in the presence of various electron donors the product THNCoA was further reduced by a two-electron reaction to most likely a conjugated hexahydro-2-naphthoyl-CoA isomer (HHNCoA). The reaction assigned to THNCoA reductase strictly depended on ATP and was oxygen-sensitive with a half-life time between 30s and 1min when exposed to air. The rate was highest with NADH as electron donor. The results indicate that two novel and completely different dearomatizing ring reductases are involved in anaerobic naphthalene degradation. While the THNCoA reducing activity shows some properties of ATP-dependent class I benzoyl-CoA reductases, NCoA reduction appears to be catalysed by a previously unknown class of dearomatizing aryl-carboxyl-CoA reductases.

Publication metadata

Author(s): Eberlein C, Johannes J, Mouttaki H, Sadeghi M, Golding BT, Boll M, Meckenstock RU

Publication type: Article

Publication status: Published

Journal: Environmental Microbiology

Year: 2013

Volume: 15

Issue: 6

Pages: 1832-1841

Print publication date: 01/06/2013

Online publication date: 22/01/2013

Acceptance date: 13/12/2012

ISSN (print): 1462-2912

ISSN (electronic): 1462-2920

Publisher: Wiley-Blackwell


DOI: 10.1111/1462-2920.12076


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Funder referenceFunder name
1319German research foundation