What is the role of the nitrate reductase (euknr) gene in fungi that live in nitrate-free environments? A targeted gene KO study in Ampelomyces mycoparasites

2021 ◽  
Author(s):  
Márk Z. Németh ◽  
Guofen Li ◽  
Diána Seress ◽  
Alexandra Pintye ◽  
Orsolya Molnár ◽  
...  
Keyword(s):  
Nitrate Reductase

Oxygen control of nitrogen oxide respiration, focusing on α-proteobacteria

2011 ◽  
Vol 39 (1) ◽  
pp. 179-183 ◽  
Author(s):  
James P. Shapleigh
Keyword(s):  
Nitrate Reductase ◽  
Nitrogen Oxide ◽  
Physiological Function ◽  
Physiological Role ◽  
Present Review ◽  
Oxygen Control ◽  
Anoxic Conditions ◽  
Periplasmic Nitrate Reductase

Denitrification is generally considered to occur under micro-oxic or anoxic conditions. With this in mind, the physiological function and regulation of several steps in the denitrification of model α-proteobacteria are compared in the present review. Expression of the periplasmic nitrate reductase is quite variable, with this enzyme being maximally expressed under oxic conditions in some bacteria, but under micro-oxic conditions in others. Expression of nitrite and NO reductases in most denitrifiers is more tightly controlled, with expression only occurring under micro-oxic conditions. A possible exception to this may be Roseobacter denitrificans, but the physiological role of these enzymes under oxic conditions is uncertain.

Dissociation of FAD from the NAD(P)H-Nitrate Reductase Complex from Ankistrodesmus braunii and Role of Flavin in Catalysis

1982 ◽  
Vol 37 (1-2) ◽  
pp. 24-30 ◽  
Author(s):  
Miguel A. De la Rosa ◽  
Antonio J. Márquez ◽  
José M. Vega
Keyword(s):  
Nitrate Reductase ◽  
Reductase Activity ◽  
Prosthetic Group ◽  
Original Activity ◽  
Enzyme Preparations ◽  
Fluorescence Studies ◽  
Transport Chain ◽  
Sulphydryl Groups ◽  
Nadh Cytochrome

Ankistrodesmus braunii NAD(P)H-nitrate reductase is a complex hemoflavomolybdoprotein composed by eight similar subunits. The flavin prosthetic group, identified as FAD, is essential for the NAD(P)H-dependent activities of the complex, and is located before the heme chromo- phore in the enzyme electron transport chain from reduced pyridine nucleotides to nitrate. Fluorescence studies indicate that nitrate reductase can dissociate about 80% of its FAD by incubation at room temperature, the flavin dissociation being followed by a parallel decrease of NADH-nitrate reductase activity. Dissociation of FAD from the protein is easily increased by dilution or prolonged dialysis of the enzyme preparations. However, exogenous FAD specifically prevents the dissociation of enzyme-bound flavin, and protects the NAD(P)H-dependent activities. The Km for FAD, as a protector of NADH-cytochrome c reductase activity, is 4 nᴍ. In addition, dithioerythritol also prevents the flavin dissociation, and therefore the presence of free sulphydryl groups in the FAD-domain is suggested. FAD-depleted nitrate reductase, obtained by several methods, is unable to recover its original activity when incubated in the presence of FAD alone or with thiols.

scholarly journals The Role of Nitrate and Ammonium Ions and Light on the Induction of Nitrate Reductase in Maize Leaves

1988 ◽  
Vol 88 (4) ◽  
pp. 1067-1072 ◽  
Author(s):  
Ann Oaks ◽  
Michel Poulle ◽  
Valerie J. Goodfellow ◽  
Leslie A. Cass ◽  
Holger Deising
Keyword(s):  
Nitrate Reductase ◽  
Ammonium Ions ◽  
Maize Leaves

A Novel Report on Assessing pH Dependent Role of Nitrate Reductase on Green Biofabrication of Gold Nanoplates and Nanocubes

2013 ◽  
Vol 7 (2) ◽  
pp. 174-180 ◽  
Author(s):  
Ashmi Mewada ◽  
Sunil Pandey ◽  
Goldie Oza ◽  
Ritu Shah ◽  
Mukeshchand Thakur ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Ph Dependent
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