Nitric oxide dioxygenation (NOD) reactions of CoIII-peroxo and NiIII-peroxo complexes: NOD versus NO activation

2020 ◽  
Vol 7 (24) ◽  
pp. 4872-4882
Author(s):  
Mahesh Yenuganti ◽  
Sandip Das ◽  
Kulbir ◽  
Somnath Ghosh ◽  
Prabhakar Bhardwaj ◽  
...  

A comparative study of “nitric oxide dioxygenation versus dioxygen or nitric oxide activation”.

2007 ◽  
Vol 282 (49) ◽  
pp. 35741-35748 ◽  
Author(s):  
Emily R. Derbyshire ◽  
Michael A. Marletta

Nitric oxide (NO) is a physiologically relevant activator of the hemoprotein soluble guanylate cyclase (sGC). In the presence of NO, sGC is activated several hundredfold above the basal level by a mechanism that remains to be elucidated. The heme ligand n-butyl isocyanide (BIC) was used to probe the mechanism of NO activation of sGC. Electronic absorption spectroscopy was used to show that BIC binds to the sGC heme, forming a 6-coordinate complex with an absorbance maximum at 429 nm. BIC activates sGC 2-5-fold, and synergizes with the allosteric activator YC-1, to activate the enzyme 15-25-fold. YC-1 activates the sGC-BIC complex, and leads to an increase in both the Vmax and Km. BIC was also used to probe the mechanism of NO activation. The activity of the sGC-BIC complex increases 15-fold in the presence of NO, without displacing BIC at the heme, which is consistent with previous reports that proposed the involvement of a non-heme NO binding site in the activation process.


2014 ◽  
Vol 3 (1) ◽  
pp. 17 ◽  
Author(s):  
Monica Verma ◽  
Kiran Dahiya ◽  
Veena Ghalaut ◽  
Abhishek Soni ◽  
Jagjeet Singh ◽  
...  

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