Results 201 to 210 of about 11,566 (244)
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Denitrification and nitrite reduction: Pseudomonas aeruginosa nitrite-reductase

Biochimie, 1984
Present knowledge of the different enzymatic steps of the denitrification chains in various bacteria, particularly Paracoccus denitrificans and Pseudomonas aeruginosa has been briefly reviewed. The question whether nitric oxide (NO), nitrous oxide (N2O) and other nitrogen derivatives are obligatory intermediates has been discussed.
Y, Henry, P, Bessières
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Nitrite Reductases in Denitrification

2007
Nitrite reductase (NIR) is a key enzyme in the dissimilatory denitrification chain, catalyzing the reduction of NO2 - to NO. Although a matter of debate for a long time, NO is now accepted product of NO2 --reduction as an obligatory intermediate in most denitrifiers, and it is further reduced to N2O by NO reductase. Purification and characterization of
RINALDO, Serena, CUTRUZZOLA', Francesca
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Octaheme nitrite reductases: Structure and properties

Biochemistry (Moscow), 2012
Octaheme oxidoreductases are widespread among various bacterial taxa involved in the biogeochemical nitrogen cycle. The evolution of octaheme oxidoreductases of the nitrogen cycle from the evolutionarily more ancient pentaheme nitrite reductases was accompanied by changes in function from reduction of nitrogen oxides to their oxidation under changing ...
T V Tikhonova, V O Popov
exaly   +3 more sources

Regulation of nitrite uptake and nitrite reductase expression in Chlamydomonas reinhardtii

Biochimica et Biophysica Acta (BBA) - General Subjects, 1991
Expression of nitrite uptake and nitrite reductase activities has been studied in Chlamydomonas reinhardtii under different nutritional conditions. Both activities were expressed at a low level in derepressed cells (with no nitrogen source) and at a high level in induced cells (with nitrate or nitrite).
A, Galván   +3 more
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Stoichiometry of nitrite reduction catalyzed by Pseudomonas aeruginosa nitrite-reductase

Biochimie, 1984
The stoichiometry of the reduction of nitrite catalyzed by Pseudomonas aeruginosa nitrite-reductase (cytochrome cd1) has been shown to yield nitrous oxide as the final product. Gas chromatography experiments demonstrated that nitric oxide is also formed as a free intermediate. A sequential formation of NO and N2O is discussed as opposed to the parallel
P, Bessières, Y, Henry
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A dissimilatory nitrite reductase in Paracoccus halodenitrificans

Archives of Microbiology, 1984
Paracoccus halodenitrificans produced a membrane-associated nitrite reductase. Spectrophotometric analysis showed it to be associated with a cd-cytochrome and located on the inner side of the cytoplasmic membrane. When supplied with nitrite, membrane preparations produced nitrous oxide and nitric oxide in different ratios depending on the electron ...
M A, Grant, L I, Hochstein
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[44] Nitrite reductase

1971
Publisher Summary This chapter discusses the determination of nitrite reductase. The usual assay involves sodium dithionite as reductant and either ferredoxin or its artificial substitute, methyl viologen, as the electron carrier. Enzymatic activity can be best followed by measuring colorimetrically the rate of disappearance of nitrite.
Manuel Losada, Antonio Paneque
openaire   +1 more source

Structure of cytochrome c nitrite reductase

Nature, 1999
The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key steps in the biological nitrogen cycle, where it participates in the anaerobic energy metabolism of dissimilatory nitrate ammonification.
Einsle, Oliver   +6 more
openaire   +4 more sources

Inheritance of Nitrite Reductase

1981
Although nitrite reductase (NiR) resides primarily in the chloroplast (Dalling et al., 1972; Lips et al., 1972; Miflin, 1974; Ritenour et al., 1967; Washitani et al., 1977) it has not been determined whether this enzyme is coded for by chloroplast DNA or by nuclear DNA.
S. Heath-Pagliuso, R. C. Huffaker
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A nitrite reductase from Neurospora crassa

Biochimica et Biophysica Acta, 1960
Abstract Nitrite reductase has been purified, over 50-fold from ordinary felts of Neurospora crassa, macroconidial wild type Em 5297a. The enzyme is a DPNH-dependent flavoprotein containing FAD, Fe and Cu and -SH groups. Copper may act by coupling the flavin component of the enzyme to nitrite since an external supply of Cu1+ reduced NO2 non ...
D J, NICHOLAS, A, MEDINA, O T, JONES
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