scholarly journals EPR spin trapping of superoxide from nitric oxide synthase

Analusis ◽  
2000 ◽  
Vol 28 (6) ◽  
pp. 487-492 ◽  
Author(s):  
J. Vásquez-Vivar ◽  
J. Joseph ◽  
H. Karoui ◽  
H. Zhang ◽  
J. Miller ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Spin Trapping ◽  
Oxide Synthase ◽  
Epr Spin Trapping

The ratio between tetrahydrobiopterin and oxidized tetrahydrobiopterin analogues controls superoxide release from endothelial nitric oxide synthase: an EPR spin trapping study

2002 ◽  
Vol 362 (3) ◽  
pp. 733-739 ◽  
Author(s):  
Jeannette VÁSQUEZ-VIVAR ◽  
Pavel MARTÁSEK ◽  
Jennifer WHITSETT ◽  
Joy JOSEPH ◽  
Balaraman KALYANARAMAN
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Spin Trapping ◽  
No Formation ◽  
Superoxide Formation ◽  
Oxide Synthase ◽  
Epr Spin Trapping ◽  
Endothelial Nitric Oxide ◽  
Superoxide Release

Augmentation of superoxide levels has been linked to impaired relaxation in hypertension, diabetes and hypercholesterolaemia. Purified endothelial nitric oxide synthase (eNOS) generates superoxide under limited availability of 5,6,7,8-tetrahydrobiopterin (BH4). Thus alterations in endothelial BH4 levels have been postulated to stimulate superoxide production from eNOS. This possibility was examined by determining the concentration-dependent effects of BH4, and its analogues, on superoxide formation by eNOS. Superoxide was quantified by EPR spin trapping, which is the only available technique to quantify superoxide from eNOS. Using 5-ethoxycarbonyl-5-methyl-pyrroline N-oxide, we show that only fully reduced BH4 diminished superoxide release from eNOS, with efficiency BH4>6-methyl-BH4>5-methyl-BH4. In contrast, partially oxidized BH4 analogues, 7,8-dihydrobiopterin (7,8-BH2) and sepiapterin had no effect. Neither l-arginine nor NG-nitro-l-arginine methyl ester (l-NAME) abolished superoxide formation. Together, BH4 and l-arginine stimulated ˙NO production at maximal rates of 148nmol/min per mg of protein. These results indicate that BH4 acts as a ‘redox switch’, decreasing superoxide release and enhancing ˙NO formation. This role was verified by adding 7,8-BH2 or sepiapterin to fully active eNOS. Both 7,8-BH2 and sepiapterin enhanced superoxide release while inhibiting ˙NO formation. Collectively, these results indicate that the ratio between oxidized and reduced BH4 metabolites tightly regulates superoxide formation from eNOS. The pathological significance of this scenario is discussed.

Spin trapping nitric oxide from neuronal nitric oxide synthase: A look at several iron–dithiocarbamate complexes

2005 ◽  
Vol 39 (10) ◽  
pp. 1027-1033 ◽  
Author(s):  
John Weaver ◽  
Supatra Porasuphatana ◽  
Pei Tsai ◽  
Theodore Budzichowski ◽  
Gerald M. Rosen
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Neuronal Nitric Oxide Synthase ◽  
Spin Trapping ◽  
Oxide Synthase

Reaction of neuronal nitric oxide synthase with the nitric oxide spin-trapping agent, iron complexed withN-dithiocarboxysarcosine

1999 ◽  
Vol 266 (3) ◽  
pp. 771-777 ◽  
Author(s):  
Hirohito Yoneyama ◽  
Hiroaki Kosaka ◽  
Taira Ohnishi ◽  
Takeshi Kawazoe ◽  
Kazuhiro Mizoguchi ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Neuronal Nitric Oxide Synthase ◽  
Spin Trapping ◽  
Oxide Synthase ◽  
Trapping Agent
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