Home - Nitrosomonas europaea - Energy.gov.
Nitrosomonas europaea. in Pure Culture. SUMMARY: Nitrosomonas europaea (Winogradsky) was isolated in pure culture from Rothamsted soil. The method used entailed: (1) building up the population of nitrifiers in enrichment cultures; (2) removal of the cells from the chalk in an enriched culture with a stream of carbon dioxide; (3) picking colonies from poured silica gel plates.
Nitrosomonas europaea Winogradsky 1892. Classification phylum Proteobacteria class Betaproteobacteria order Nitrosomonadales family. Nitrosomonas species Nitrosomonas europaea.
Nitrosomonas eutropha C91 ( eu -, good; trophos, one who feeds) (also known as strain Nm57; formerly ATCC 25984, which is no longer available) is a Gram-negative betaproteobacterium closely related to the better studied Nitrosomonas europaea (Chain, 2001-2009).
Nitrosomonas europaea is a Gram-negative obligate chemolithoautotroph that can derive all its energy and reductant for growth from the oxidation of ammonia to nitrite and lives in several places such as soil, sewage, freshwater, the walls of buildings and on the surface of monuments especially in polluted areas where the air contains high levels of nitrogen compounds.
Information on the name and the taxonomic classification. Name and taxonomic classification; Last LPSN update: 31-03-2020 (DD-MM-YYYY) Domain: Bacteria: Phylum: Proteobacteria: Class: Betaproteobacteria: Order:. Nitrosomonas europaea gene for 16S rRNA, partial sequence, strain: ATCC25978: AB070982. ENA. 16S: 1373: 915 tax ID: Availability in.
The effects of trichloromethyl-1, 3, 5-triazines on the ammonia oxidizing activity of the nitrifying bacteria Nitrosomonas europaea ATCC 25978 and Nitrosomonas sp. TK 794 were investigated.
Here we report the first structure of an Rh family member, the Rh protein from the chemolithoautotrophic ammonia-oxidizing bacterium Nitrosomonas europaea. This Rh protein exhibits a number of similarities to its Amt cousins, including a trimeric oligomeric state, a central pore with an unusual twin-His site in the middle, and a Phe residue that blocks the channel for small-molecule transport.