Results 161 to 170 of about 5,332 (201)
Some of the next articles are maybe not open access.
Anaerobic metabolism of Nitrosomonas europaea
Archives of Microbiology, 1992Nitrosomonas europaea is capable of maintaining an anaerobic metabolism, using pyruvate as an electron donor and nitrite as an electron acceptor; utilization of nitrite depends upon supply of both pyruvate and ammonia. The role of ammonia in this reaction was not determined.
Aharon Abeliovich, Ahuva Vonshak
openaire +3 more sources
Chemoorganoheterotrophic Growth of Nitrosomonas europaea and Nitrosomonas eutropha
Current Microbiology, 2009The ammonia oxidizers Nitrosomonas europaea and Nitrosomonas eutropha are able to grow chemoorganotrophically under anoxic conditions with pyruvate, lactate, acetate, serine, succinate, alpha-ketoglutarate, or fructose as substrate and nitrite as terminal electron acceptor.
openaire +4 more sources
Ethylene oxidation by Nitrosomonas europaea
Archives of Microbiology, 1984Incubation of whole cells of the nitrifying bacterium Nitrosomonas europaea with ethylene led to the formation of ethylene oxide. Ethylene oxide production was prevented by inhibitors of ammonium ion oxidation, and showed properties implying that ethylene is a substrate for the ammonia oxidising enzyme, ammonia monooxygenase.
Michael R. Hyman, Paul M. Wood
openaire +1 more source
Inhibition of biofilm populations of Nitrosomonas europaea
Microbial Ecology, 1992The influence of surface attachment and growth on inhibition of the ammonia oxidizing bacterium, Nitrosomonas europaea, by nitrapyrin was investigated in liquid culture in the presence and absence of glass slides. Significant attachment to glass slides occurred in the absence of ammonia, but the extent of attachment was not affected by nitrapyrin, nor ...
S J, Powell, J I, Prosser
openaire +2 more sources
Secondary transport of amino acids in Nitrosomonas europaea
Archives of Microbiology, 1992Nitrosomonas europaea is capable of incorporating exogenously supplied amino acids. Studies in whole cells revealed that at least eight amino acids are actively accumulated, probably by the action of three different transport systems, each with high affinity (mu-molar range) for several amino acids.
Frijlink, M.J. +4 more
openaire +3 more sources
Ammonia Monooxygenase from Nitrosomonas europaea
1996Nitrosomonas europaea is an obligate chemolithoautotroph which obtains energy for growth from the oxidation of ammonia (NH3) to nitrite (NO2 -). This bacterium, along with other bacteria which obtain their energy from the oxidation of NH3, contribute to the biogeochemical cycling of inorganic nitrogen.
D. J. Arp +6 more
openaire +1 more source
Dinitrogen production from ammonia by Nitrosomonas europaea
Applied Catalysis A: General, 2002Abstract In this study, the conversion efficiency and optimal conditions of successive nitrification and denitrification were assessed for Nitrosomonas europaea , which uses ammonia monooxygenase (AMO), nitrite reductase and nitrous oxide reductase. In aerobic conditions, the first step of nitrification (i.e.
N. K. Shrestha +3 more
openaire +1 more source
Dissecting Iron Uptake and Homeostasis in Nitrosomonas europaea
2011The chemolithoautotroph Nitrosomonas europaea oxidizes about 25 mol of NH(3) for each mole of CO(2) that is converted to biomass using an array of heme and nonheme Fe-containing proteins. Hence mechanisms of efficient iron (Fe) uptake and homeostasis are particularly important for this Betaproteobacterium. Among nitrifiers, N.europaea has been the most
Luis A, Sayavedra-Soto +2 more
openaire +2 more sources
EPR of hydroxylamine oxidoreductase from Nitrosomonas europaea
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1981Abstract EPR spectra are reported for the multiheme enzyme hydroxylamine oxidoreductase of Nitrosomonas europaea. Signals arising from several different types of low-spin ( S = 1 2 ) ferric heme were observed in the resting (oxidized) enzyme, but no evidence was obtained for high-spin ( S = 5 2 ) heme, copper or iron-sulfur centers ...
Larry E. Vickery, Alan B. Hooper
openaire +1 more source
A ‘blue’ copper oxidase from Nitrosomonas europaea
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985Abstract A soluble copper-containing protein with p -phenylenediamine oxidase activity was purified from Nitrosomonas europaea by flat-bed isoelectric focusing and chromatography on Sephacryl S-300. The native and subunit molecular weights were 127 500 and 40 100, respectively; the isoelectric point was pH 4.63.
Alan A. DiSpirito +3 more
openaire +1 more source