The Identification of the Pterin-Binding Domain in the Nitric Oxide Synthase′s Sequence

1995 ◽  
Vol 206 (2) ◽  
pp. 736-741 ◽  
Author(s):  
V.Y. Uvarov ◽  
A.A. Lyashenko
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Binding Domain ◽  
Oxide Synthase

scholarly journals Crystal Structure of the FAD/NADPH-binding Domain of Rat Neuronal Nitric-oxide Synthase

2001 ◽  
Vol 276 (40) ◽  
pp. 37506-37513 ◽  
Author(s):  
Jian Zhang ◽  
Pavel Martàsek ◽  
Rosemary Paschke ◽  
Thomas Shea ◽  
Bettie Sue Siler Masters ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Neuronal Nitric Oxide Synthase ◽  
Binding Domain ◽  
Oxide Synthase

scholarly journals Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase

2013 ◽  
Vol 450 (3) ◽  
pp. 607-617 ◽  
Author(s):  
Mohammad Mahfuzul Haque ◽  
Mekki Bayachou ◽  
Mohammed A. Fadlalla ◽  
Deborah Durra ◽  
Dennis J. Stuehr
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Conformational Transition ◽  
Electron Flux ◽  
Conformational State ◽  
Binding Domain ◽  
Slow Electron ◽  
Pairing Interactions ◽  
Oxygenase Domain ◽  
Oxide Synthase

The NOS (nitric oxide synthase; EC 1.14.13.39) enzymes contain a C-terminal flavoprotein domain [NOSred (reductase domain of NOS)] that binds FAD and FMN, and an N-terminal oxygenase domain that binds haem. Evidence suggests that the FMN-binding domain undergoes large conformational motions to shuttle electrons between the NADPH/FAD-binding domain [FNR (ferredoxin NADP-reductase)] and the oxygenase domain. Previously we have shown that three residues on the FMN domain (Glu762, Glu816 and Glu819) that make charge-pairing interactions with the FNR help to slow electron flux through nNOSred (neuronal NOSred). In the present study, we show that charge neutralization or reversal at each of these residues alters the setpoint [Keq(A)] of the NOSred conformational equilibrium to favour the open (FMN-deshielded) conformational state. Moreover, computer simulations of the kinetic traces of cytochrome c reduction by the mutants suggest that they have higher conformational transition rates (1.5–4-fold) and rates of interflavin electron transfer (1.5–2-fold) relative to wild-type nNOSred. We conclude that the three charge-pairing residues on the FMN domain govern electron flux through nNOSred by stabilizing its closed (FMN-shielded) conformational state and by retarding the rate of conformational switching between its open and closed conformations.

The calmodulin binding domain of nitric oxide synthase and adenylyl cyclase

Biochemistry ◽  
1993 ◽  
Vol 32 (23) ◽  
pp. 6081-6088 ◽  
Author(s):  
Thomas Vorherr ◽  
Lea Knoepfel ◽  
Francesco Hofmann ◽  
Stefan Mollner ◽  
Thomas Pfeuffer ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Adenylyl Cyclase ◽  
Binding Domain ◽  
Calmodulin Binding ◽  
Oxide Synthase

scholarly journals Interaction of Calmodulin with Its Binding Domain of Rat Cerebellar Nitric Oxide Synthase

1995 ◽  
Vol 270 (36) ◽  
pp. 20901-20907 ◽  
Author(s):  
Mingjie Zhang ◽  
Tao Yuan ◽  
James M. Aramini ◽  
Hans J. Vogel
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Binding Domain ◽  
Oxide Synthase
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