The Isolation of Nitrosomonas europaea in Pure Culture

The isolation of Nitrosomonas europaea in pure culture.

Isolation of Nitrosomonas in pure culture.

Although it has been 68 years since Winogradsky (1890) accomplished the first isolation of nitrifying bacteria, the methods employed have not been improved significantly, and pure cultures remain incredibly difficult to obtain. The literature records numerous attempts to secure Nitrosomonas in pure culture. Nevertheless, the organism has seldom been isolated by dilution techniques. In the relat...

Methane oxidation by Nitrosomonas europaea.

Methane inhibited NH4+ utilization by Nitrosomonas europaea with a Ki of 2mM. O2 consumption was not inhibited. In the absence of NH4+, or with hydrazine as reductant, methane caused nearly a doubling in the rate of O2 uptake. The stimulation was abolished by allylthiourea, a sensitive inhibitor of the oxidation of NH4+. Analysis revealed that methanol was being formed in these experiments, wit...

Structure of the Nitrosomonas europaea Rh protein.

Amt/MEP/Rh proteins are a family of integral membrane proteins implicated in the transport of NH3, CH(2)NH2, and CO2. Whereas Amt/MEP proteins are agreed to transport ammonia (NH3/NH4+), the primary substrate for Rh proteins has been controversial. Initial studies suggested that Rh proteins also transport ammonia, but more recent evidence suggests that they transport CO2. Here we report the fir...

Cytochrome aa3 from Nitrosomonas europaea.

Cytochrome c oxidase has been purified from the ammonia oxidizing chemoautotroph Nitrosomonas europaea by ion-exchange chromatography in the presence of Triton X-100. The enzyme has absorption maxima at 420 and 592 nm in the resting state and at 444 and 598 nm in the dithionite-reduced form; optical extinction coefficient (598 nm minus 640 nm) = 21.9 cm-1 nM-1. The enzyme has approximately 11 n...