Activators of the nitric oxide sensor, soluble guanylate cyclase

2000 ◽  
Vol 10 (11) ◽  
pp. 1765-1770 ◽  
2005 ◽  
Vol 513 (1-2) ◽  
pp. 67-74 ◽  
Author(s):  
Peter M. Schmidt ◽  
Christiane Rothkegel ◽  
Frank Wunder ◽  
Henning Schröder ◽  
Johannes-Peter Stasch

2010 ◽  
Vol 28 (8) ◽  
pp. 1666-1675 ◽  
Author(s):  
Yuliya Sharkovska ◽  
Philipp Kalk ◽  
Bettina Lawrenz ◽  
Michael Godes ◽  
Linda Sarah Hoffmann ◽  
...  

1997 ◽  
Vol 320 (2-3) ◽  
pp. 161-166 ◽  
Author(s):  
Che-Ming Teng ◽  
Chin-Chung Wu ◽  
Feng-Nien Ko ◽  
Fang-Yu Lee ◽  
Sheng-Chu Kuo

Nitric Oxide ◽  
2006 ◽  
Vol 14 (4) ◽  
pp. 4-5
Author(s):  
Patrick Yves Sips ◽  
Emmanuel Buys ◽  
Elke Rogge ◽  
Sofie Nimmegeers ◽  
Mieke Dewerchin ◽  
...  

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Kimberly Long ◽  
Kim Tang ◽  
Renee Sarno ◽  
Rob Solinga ◽  
Jaime Masferrer

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.


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