Novel degradative pathway of 4-nitrobenzoate in Comamonas acidovorans NBA-10.

Abstract

A Comamonas acidovorans strain, designated NBA-10, was isolated on 4-nitrobenzoate as sole carbon and energy source. When grown on 4-nitrobenzoate, it was simultaneously adapted to 4-nitrosobenzoate and 4-hydroxylaminobenzoate but not to 4-hydroxybenzoate or 4-aminobenzoate. In cell extracts with NADPH present, 4-nitrobenzoate was degraded to 4-hydroxylaminobenzoate and 3,4-dihydroxybenzoate. Partial purification of the 4-nitrobenzoate reductase revealed that 4-nitrobenzoate is degraded via 4-nitrosobenzoate to 4-hydroxylamino-benzoate. The substrate specificity of the enzyme was narrow and NADPH was 15 times more effective as a cofactor than NADH. The results provide evidence for a novel pathway for aerobic degradation of 4-nitrobenzoate, since neither 4-hydroxybenzoate nor 4-aminobenzoate were involved in the degradative pathway.

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@article{Groenewegen1992NovelDP, title={Novel degradative pathway of 4-nitrobenzoate in Comamonas acidovorans NBA-10.}, author={Peter E. J. Groenewegen and Peter Breeuwer and Joop M.L.M. van Helvoort and Alette A M Langenhoff and Frank de Vries and Jan A. M. de Bont}, journal={Journal of general microbiology}, year={1992}, volume={138 Pt 8}, pages={1599-605} }