PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Nitrobacter”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1976

Growth of nitrobacter in the presence of organic matter. II. Chemoorganotrophic growth of Nitrobacter agilis.

1. After a resting period of up to 6 months cells of Nitrobacter agilis grow with acetate, formate, and pyruvate as carbon and energy source. Yeast extract and peptone were added to supply the organism with nitrogen and to meet possible vitamin requirements. 2. The length of the growth period depends on the substrate; it increases according to the following sequence: pyruvate, formate, acetate. The highest growth yield is observed with pyruvate, the lowest with formate. 3. O2 consumption is increased in the presence of substrates as compared to endogenous respiration. With pyruvate and acetate twice as much O2 is consumed, with formate 7 times, with yeast extractpeptone 10 times as much. 4. The ability of nitrite oxidation is largely preserved, except in cells grown with acetate or pyruvate in the presence of 0.015% yeast extract and peptone. Such cells have nearly no cytochrome a1. Accordingly. the cytochrome spectra of nitrite oxidizers grown under chemoorganotrophic and lithoautotrophic conditions coincide qualitatively. 5. The nitrite oxidizing system is inducible. It is induced by nitrite but also by substances present in yeast extract and peptone. Cells grown on acetate and yeast extract and peptone (0.015%) require 3--4 weeks before they regain the ability to grow with nitrite. Cells grown chemoorganotrophically with the same substrates and yeast extract and peptone (0.15%) start growing and nitrite as energy source without a lag. 6. Cell size and form, distribution of storage materials, order and fine structure of double membranes are correlated with growth conditions.

Acetates↗
PubMed1976

Growth of Nitrobacter in the presence of organic matter. I. Mixotrophic growth.

1. Culture filtrates of heterotrophic bacteria were tested for their stimulatory effect on nitrification of three strains of Nitrobacter. 2. Yeast extract-peptone solution, in which Pseudomonas fluorescens had grown, after removal of the cells was added to autotrophically growing cultures of Nitrobacter agilis; it caused a stimulated nitrite oxidation and growth of Nitrobacter agilis. 3. The degree of stimulation depended on: a) the proportion of the culture filtrate to the autotrophic medium; b) the composition of the complex medium in which Pseudomonas fluorescens had been grown; c) the time the heterotrophic bacterium had been grown in the complex medium. 4. The stimulatory effect was highest with Nitrobacter agilis, less with Nitrobacter winogradskyi and negligible with Nitrobacter K4. 5. It was possible to adapt nutrifying cells of Nitrobacter agilis to higher concentrations of yeast extract and peptone. After the nitrite had been completely oxidized the cell-N still increased up to 30% before growth stopped.

Culture Media↗
PubMed1975

Autoradiography and immunofluorescence combined for autecological study of single cell activity with Nitrobacter as a model system.

Specific detection of a particular bacterium by immunofluorescence was combined with estimation of its metabolic activity by autoradiography. The nitrifying bacteria Nitrobacter agilis and N. winogradskyi were used as a model system. Nitrobacter were incubated with NaH14CO3 and 14CO2 prior to study. The same preparations made for autoradiograms were stained with fluorescent antibodies specific for the Nitrobacter species. Examination by epifluorescence and transmitted dark-field microscopy revealed Nitrobacter cells with and without associated silver grains. Direct detection and simultaneous evaluation of metabolic activity of Nitrobacter was demonstrated in pure cultures, in a simple mixed culture, and in a natural soil.

Autoradiography↗
PubMed1992

Characterization of natural populations of Nitrobacter spp. using PCR/RFLP analysis of the ribosomal intergenic spacer.

DNA sequences from the intergenic spacer (IGS) region of the ribosomal operon were amplified by the polymerase chain reaction (PCR) technique using two primers derived from 16S and 23S rRNA conserved sequences. The PCR products, cleaved by 4 base cutting restriction enzymes, were used to differentiate Nitrobacter strains. This method offered a convenient alternative to serological testing for characterization of Nitrobacter isolates and enabled a large number of strains to be genotypically characterized easily and rapidly. This method was successfully used to characterize natural populations of Nitrobacter from various soils and a lake. A diversity was demonstrated in various soils, and in a lake both in freshwater and in sediments. Strains closely related to both WL and LL were found in these ecosystems. It seems that the diversity of Nitrobacter populations was not associated with global environments but may be related to the presence of locally coexisting niches.

Base Sequence↗
PubMed1977

Phosphoribulokinase from Nitrobacter winogradskyi: activation by reduced nicotinamide adenine dinucleotide and inhibition by pyridoxal phosphate.

CO2 fixation by particle-free extracts from Nitrobacter winogradskyi increased by addition of reduced nicotinamide adenine dinucleotide (NADH). Ribulose-1,5-diphosphate, however, increased CO2 fixation, even in the absence of NADH. Phosphoribulokinase (EC 2.7.1.19) was the enzyme of Nitrobacter extracts that was activated specifically by NADH. Pyridoxal-5-phosphate inhibited both CO2 fixation and NADH-activated phosphoribulokinase from Nitrobacter. However, it did not affect phosphoribulokinase from spinach leaves. Since the spinach enzyme had also no requirement for reduced pyridine nucleotides, it appears that pyridoxal phosphate interferes only with the binding of NADH and not with the binding of ribulose-5-phosphate and adenosine-5'-triphosphate. The regulation of phosphoribulokinase activity by NADH provided Nitrobacter with an energy-dependent control mechanism of CO2 assimilation.

Carbon Dioxide↗
PubMed1977

Immunofluorescence studies of Nitrobacter populations in soils.

Certain steps of a protocol to enumerate a bacterium directly in soil by immunofluorescence were studied with respect to the enumeration of Nitrobacter in soils of diverse properties. Maximal counts of Nitrobacter were obtained by varying factors involved in the release of bacteria from the soil. Differences with respect to these factors were related to soil-colloidal properties. Enumeration protocols modified with regard to soil properties were used with strain-specific fluorescent antibodies (FA) to enumerate Nitrobacter populations (a) in soil during storage, (b) in comparison with most probable number (MPN) enumeration, and (c) occurring in a spectrum of soil samples. FA counting was rapid and precise and gave counts generally 10- to 100-fold higher than obtained by MPN. Nitrobacter cells of the two serotypes studied, designated as agilis and Winogradsky, occurred in each soil at levels of 10(4)-10(5) per gram.

Bacteriological Techniques↗
PubMed1976

Lipids of Nitrobacter and effects of cultural conditions on fatty acid composition.

The nitrite-oxidizing autotroph, Nitrobacter was studied with respect to fatty acid composition and lipids. One fatty acid, shown to be cis-11-actadecenoic acid (cis-vaccenic) accounted for almost 96% of the total fatty acids of the extractable lipids of Nitrobacter agilis, Nitrobacter winogradskyi and each of several isolates from Minnesota and Moroccan soils studied. The cis-vaccenic acid was high in all organisms, ranging from 85 to 95% when grown at 27degreesC in the log growth phase, the other major acid was plamitic (16 : 1). All converted ces-vaccenic acid to a 19-carbon cyclopropanecarboxylic acid upon entering the stationary growth phase. The 11-carbon cyclopropanecarboxylic acid was not degraded when stationary phase cells were reinoculated into fresh medium. In N. agilis the levels of cis-vaccenic acid ranged from 86.8% when grown at 33degreesC to 95.6% when grown at 19degreesC. Addition of acetate or casein hydrolyzate to the inorganic medium had virtually no effect on the fatty acid composition of N. agilis, while propionate effected both qualitative and quantitative changes. In all organisms phosphatidylcholine made up a large portion of the extractable lipids. The distribution was phosphatidylcholine, 54%; phosphatidylethanolamine, 23%; phosphatidylglycerol, 10%; and neutral lipids, 11% for N. agilis.

Carboxylic Acids↗
PubMed1974

Autecological study of the chemoautotroph Nitrobacter by immunofluorescence.

Fluorescent antibodies (FA) prepared for Nitrobacter agilis and N. winogradskyi were highly reactive in homologous staining. Low-level cross-reactions between the two species were removed by adsorption. All 15 pure-culture isolates of Nitrobacter tested reacted strongly with either N. agilis FA or N. winogradskyi FA. All pure-culture isolates from soils were determined to be N. winogradskyi; those from Mammoth Cave sediments and a cattle waste oxidation ditch were N. agilis. No cross-reaction was found in extensive tests that included five isolates of Nitrosomonas europaea and 668 heterotrophic aerobic and anaerobic bacteria isolated from soil, sewage, and cave sites. The FA preparations were used to detect Nitrobacter species in Mammoth Cave sediments, in a cattle waste oxidation ditch, and in surface waters and sediments of a river and to observe that N. winogradskyi can outgrow N. agilis in enrichment culture.

Aerobiosis↗
PubMed1975

Study of the regulation of oxidation and CO2 assimilation in intact Nitrobacter winogradskyi cells.

1. Changes of the adenine nucleotides in resting and growing Nitrobacter winogradskyi cells were measured in connection with regulating processes during nitrite oxidation and endogenous respiration. 2. After the addition of nitrite to endogenously respiring cells the ATP pool increased strongly during the first 60 sec at the expense of the ADP pool. At this point the energy charge was approx. 0.55. After the first 90 sec the ATP pool dropped, oscillating, to a lower level. The CO2 assimilation began at this point. 3. Under a nitrogen atmosphere the AMP pool increased and the ATP pool decreased. With a value of approx. 0.17 the energy charge was extremely low. When oxygen was added the Nitrobacter cells began to oxidize stored NADH. The ATP pool increased in a few seconds whereas the AMP pool decreased. The P/O ratio of endogenously respiring cells equaled 0.6 under these conditions. 4. During the changeover from anaerobic to aerobic conditions and in the presence of nitrite the nitrite oxidation and CO2 assimilation, opposed to aerobic conditions, were inhibited at first after the nitrite addition. The changeover of the respiratory chain enzymes from a reduced to an oxidized charge and the ATP increase were delayed in comparison with experiments without nitrite. According to these findings the endogenous respiration must be almost nil while nitrite oxidizing cells are growing.

Adenine Nucleotides↗
PubMed1969

Nitrite oxidase and nitrate reductase in Nitrobacter agilis.

Nitrite oxidase and nitrate reductase in Nitrobacter agilis were shown to be separate enzymes. The best separation of the two systems was achieved by ammonium sulphate fractionation. The effects of various compounds, including antimycin A, 2-n-heptyl-4-hydroxyquinoline N-oxide and chlorate, also clearly distinguish between the two enzyme reactions. The relationship between the two opposing reactions in Nitrobacter is discussed.

Antimycin A↗
PubMed1970

Effects of pesticides on nitrite oxidation by Nitrobacter agilis.

The influence of pesticides on the growth of Nitrobacter agilis in aerated cultures and on the respiration of N. agilis cell suspensions and cell-free extracts was studied. Two pesticides, aldrin and simazine, were not inhibitory to growth of Nitrobacter, but five compounds [isopropyl N-(3-chlorophenyl) carbamate (CIPC), chlordane, 1,1-dichloro-2,2-bis (p-chlorophenyl) ethane (DDD), heptachlor, and lindane] prevented growth when added to the medium at a concentration of 10 mug/ml. Whereas CIPC and eptam prevented nitrite oxidation by cell suspensions, the addition of DDD and lindane resulted in only partial inhibition of the oxidation. Heptachlor and chlordane also caused only partial inhibition of oxidation, but were more toxic with cell-free extract nitrite oxidase. None of the pesticides inhibited the nitrate reductase activity of cell-free extracts, but most caused some repression of cytochrome c oxidase activity. Heptachlor was the most deleterious compound.

Bacterial Proteins↗
PubMed1979

Deoxyribonucleic acid in Nitrobacter carboxysomes.

Carboxysomes were isolated from Nitrobacter winogradskyi and Nitrobacter agilis. The icosahedral particles contained double-stranded deoxyribonucleic acid (DNA). In the presence of ethidium bromide and cesium chloride, the particle-bound DNA had a buoyant density of rho 25 = 1.701 g/cm3. Electron microscopy revealed the DNA to be a 14-micron circular molecule.

Centrifugation, Density Gradient↗
PubMed1977

Enzymatic studies on autotrophically, mixotrophically and heterotrophically grown Nitrobacter agilis with special reference to nitrite oxidase.

Nitrobacter agilis was grown autotrophically on nitrite, mixotrophically on nitrite together with either acetate or pyruvate and heterotrophically on acetate and casamino acids, pyruvate and casamino acids or pyruvate and nitrate. The enzymatic activities differed most in the key enzymes of lithotrophic metabolism. Nitrite oxidase was repressed 90% in 10 days after transition to heterotrophic growth and was no longer detectable after several transfers. The induction of nitrite oxidase began after a lag of 2 days and reached the autotrophic level after 7 days when pyruvate was the carbon and energy source and after 9 days using acetate.

Acetates↗
PubMed1975

Adenine nucleotide pool variations in intact Nitrobacter winogradskyi cells.

1. The ATP pool in Nitrobacter winogradskyi cells was determined by means of the luciferin-luciferase enzyme system and the ADP and AMP pools were measured after enzymatic conversion into ATP. 2. In the first 10 min after addition of nitrite to endogenously respiring cells, which had stood for 5--16 days after completion of the nitrite oxidation, the ATP pool dropped about 60%. 3. During the log phase the ATP pool was approx. 20--40 pmoles/5 mug cell-N. During growth it increased exponentially by 3--4 times the amount until the nitrite had been used up. Subsquently the ATP pool decreased at first rapidly and then more slowly without sinking to 0 in the first 2 months after nitrification. 4. Nitrite oxidizing cells had an energy charge of 0.37 during the log-phase. After approx. 90% of the substrate had been used up the energy charge had reached 0.57. 5. If the CO2 assimilation was inhibited in growing cultures by increased oxygen partial pressure, nitrite oxidation continued but the ATP pool increased. 6. The ATP pool and the activity of the endogenous respiration decreased by more than 50% during the first hours after the substrate had been used up.

Adenine Nucleotides↗
PubMed1984

A relationship between prokaryote and eukaryote observed in Nitrobacter agilis cytochromes AA3 and C.

Cytochrome aa3 (cytochrome c oxidase) and cytochrome c were purified from Nitrobacter agilis, and some of their properties were compared with those of the respective counterparts of eukaryote from the evolutionary point of view. N. agilis cytochrome aa3 has many functional and structural properties similar to those of eukaryotic cytochrome aa3, although its molecule is composed of only two kinds of subunits unlike the eukaryotic cytochrome which is composed of 7 kinds of subunits. N. agilis cytochrome c is homologous to eukaryotic cytochrome c; 50 amino acid residues of the bacterial cytochrome c are identical with those of horse cytochrome c. It reacts with yeast cytochrome c peroxidase as rapidly as eukaryotic cytochrome c does. So far as based on the molecular features of cytochromes aa3 and c, N. agilis appears to be one of the organisms which may link in evolution prokaryote to eukaryote.

Amino Acid Sequence↗
PubMed1988

The nitrite oxidizing system of Nitrobacter winogradskyi.

Cytochrome components which participate in the oxidation of nitrite in Nitrobacter winogradskyi have been highly purified and their properties studied in detail. Cytochrome a1c1 is an iron-sulphur molybdoenzyme which has haems a and c and acts as a nitrite-cytochrome c oxidoreductase. Cytochrome c-550 is homologous to eukaryotic cytochrome c and acts as the electron mediator between cytochrome a1c1 and aa3-type cytochrome c oxidase. The oxidase is composed of two kinds of subunits, has two molecules of haem a and two atoms of copper in the molecule, and oxidizes actively eukaryotic ferrocytochrome c as well as its own ferrocytochrome c-550. Further, a flavoenzyme has been obtained which has transhydrogenase activity and catalyses reduction of NADP+ with benzylviologen radical. This enzyme may be responsible for production of NADPH in N. winogradskyi. The electron transfer against redox potential from NO2- to cytochrome c could be pushed through prompt removal by cytochrome aa3 of H+ formed by the dehydrogenation of NO2- + H2O. As cytochrome c in anaerobically kept cell-free extracts is rapidly reduced on addition of NO2-, a membrane potential does not seem necessary for the reduction of cytochrome c by cytochrome a1c1 with NO2- in vivo.

Amino Acid Sequence↗
PubMed1991

Purification and characterization of ATPase from Nitrobacter winogradskyi.

An ATPase was purified from Nitrobacter winogradskyi, and some of its molecular and enzymatic properties were determined. The enzyme was composed of two subunits of 64 and 59 kDa, respectively. The enzyme had its pH optimum at 9.5 and showed a specific activity of 7 units per mg protein. This activity was about 14% and 18% of that of F1-ATPases obtained from Escherichia coli and Sulfolobus acidocaldarius, respectively. The enzyme was 29% and 6% inhibited by 100 microM dicyclohexylcarbodiimide (DCCD) and 100 microM NaN3, respectively. It was not inhibited by 20 mM NaNO3.

Adenosine Triphosphatases↗