Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea

Abstract

Nitrosomonas europaea uses only NHi3, CO2 and mineral salts for growth and as such it is an obligate chemo-lithoautotroph. The oxidation of NH3 is a two-step process catalyzed by ammonia monooxygenase (AMO) and hydroxylamine oxidoreductase (HAO). AMO catalyzes the oxidation of NH3 to NH2OH and HAO catalyzes the oxidation of NH2OH to NO2-. AMO is a membrane-bound enzyme composed of three subunits. HAO is located in the periplasm and is a homotrimer with each subunit containing eight c-type hemes. The electron flow from HAO is channeled through cytochrome c554 to cytochrome cm552, where it is partitioned for further utilization. Among the ammonia-oxidizing bacteria, the genes for AMO, these cytochromes, and HAO are present in up to three highly similar copies. Mutants with mutations in the copies of amoCAB and hao in N. europaea have been isolated. All of the amoCAB and hao gene copies are functional. N. europaea was selected by the United States Department of Energy for a whole-genome sequencing project. In this article, we review recent research on the molecular biology and biochemistry of NH3 oxidation in nitrifiers.