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Performance of aerobic granular sludge for piggery wastewater treatment and its Cu²⁺ and Zn²⁺ removal mechanism. [PDF]

Appl Microbiol Biotechnol
Wang X, Xiao S, Li M, Wang B, Zhou X, Zhou Y, Chen Z, Zhang X.   +7 more
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Chemoorganoheterotrophic Growth of Nitrosomonas europaea and Nitrosomonas eutropha

Current Microbiology, 2009
The 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.
exaly   +3 more sources

Quainification and Characterisation of Nitrosomonas and Nitrobacter Using Monoclonal Antibodies

Water Science and Technology, 1994
Nitrobacter and Nitrosomonas were isolated in pure cultures from two large waste water treatment plants in the Stockholm area. Using the hybridoma technique, monoclonal antibodies were produced specific for Nitrobacter and Nitrosomonas respectively ...
B. Sandén, C. Grunditz, Y. Hansson, G. Dalhammar   +3 more
exaly   +2 more sources

The transcription of the cbb operon in Nitrosomonas europaea

Microbiology, 2004
Nitrosomonas europaeais an aerobic ammonia-oxidizing bacterium that participates in the C and N cycles.N. europaeautilizes CO2as its predominant carbon source, and is an obligate chemolithotroph, deriving all the reductant required for energy and biosynthesis from the oxidation of ammonia (NH3) to nitrite ().
Xueming, Wei, Luis A, Sayavedra-Soto, Daniel J, Arp   +2 more
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Inhibition of biofilm populations of Nitrosomonas europaea

Microbial Ecology, 1992
The 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
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A Physiological and Genomic Comparison of Nitrosomonas Cluster 6a and 7 Ammonia-Oxidizing Bacteria [PDF]

Microbial Ecology, 2019
Ammonia-oxidizing bacteria (AOB) within the genus Nitrosomonas perform the first step in nitrification, ammonia oxidation, and are found in diverse aquatic and terrestrial environments.
Lisa Y Stein, Annette Bollmann, Martin Gunter Klotz   +2 more
exaly   +2 more sources

Secondary transport of amino acids in Nitrosomonas europaea

Archives of Microbiology, 1992
Nitrosomonas 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., Abee, T., Laanbroek, H.J., de Boer, W., Konings, W.N.   +4 more
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Anaerobic metabolism of Nitrosomonas europaea

Archives of Microbiology, 1992
Nitrosomonas 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
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Exploring nitrifier denitrification in Nitrosomonas communis and Nitrosomonas europaea through physiology and proteomic analysis

2023
The current understanding of how ammonia oxidizing bacteria (AOB) produce the potent greenhouse gas nitrous oxide is incomplete and inaccurate since most studies are focused on the model organism for the group, Nitrosomonas europaea, which does not represent the physiological diversity of AOB.
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Ethylene oxidation by Nitrosomonas europaea

Archives of Microbiology, 1984
Incubation 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
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