Finding a new pathway for acid-induced nitrite reduction reaction: formation of nitric oxide with hydrogen peroxide

2019 ◽  
Vol 48 (37) ◽  
pp. 13916-13920 ◽  
Author(s):  
Mohammed Ajmal Puthiyaveetil Yoosaf ◽  
Somnath Ghosh ◽  
Yatheesh Narayan ◽  
Munendra Yadav ◽  
Subash Chandra Sahoo ◽  
...  

Here, we report a new pathway for nitrite reduction chemistry, formation of cobalt-nitrosyl ({CoII-NO}8) with H2O2 in the reaction of a CoII-nitrito complex with a one-fold acid (H+) via the formation of a CoII-nitrous acid intermediate ({CoII-ONOH}).

1891 ◽  
Vol 48 (292-295) ◽  
pp. 458-459 ◽  

This paper is in continuation of a preliminary communication on the same subject; the main points contained in it are as follows: I. The metals copper, mercury, and bismuth do not dissolve in nitric acid of about 30 per cent, concentration (the acid commonly employed for the preparation of nitric oxide gas) and heated to a temperature of 30ºC., provided that nitrous acid is neither present initially nor formed subsequently. To prevent this, it is nocessary in the cases of copper and bismuth to add a small quantity of some oxidising substance, such as hydrogen peroxide or potassium chlorate, or, as less efficacious, potassium permanganate, or to pass a current of air or, lastly, such a substance as urea, which destroys the nitrous acid by its interaction.


2013 ◽  
Vol 31 (3) ◽  
pp. 278
Author(s):  
Wen-Qi XIE ◽  
Jin-Ping ZHANG ◽  
Jian-Yi TAN ◽  
Xiao-Li XUAN ◽  
Yong-Fei WANG ◽  
...  

2002 ◽  
Vol 53 (372) ◽  
pp. 1237-1247 ◽  
Author(s):  
Steven J. Neill ◽  
Radhika Desikan ◽  
Andrew Clarke ◽  
Roger D. Hurst ◽  
John T. Hancock

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
Heather J. Montgomery ◽  
Andrea L. Dupont ◽  
Hilary E. Leivo ◽  
J. Guy Guillemette

The nitric oxide synthase-like protein fromBacillus cereus(bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine andNG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation ofNG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.


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