@article{mbs:/content/journal/micro/10.1099/00221287-138-8-1599, author = "Groenewegen, Peter E. J. and Breeuwer, Pieter and van Helvoort, Joop M. L. M. and Langenhoff, Alette A. M. and de Vries, Floris P. and de Bont, Jan A. M.", title = "Novel degradative pathway of 4-nitrobenzoate in Comamonas acidovorans NBA-10", journal= "Microbiology", year = "1992", volume = "138", number = "8", pages = "1599-1605", doi = "https://doi.org/10.1099/00221287-138-8-1599", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-138-8-1599", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", 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-hydroxylaminobenzoate. 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.", }