Dissecting mechanism of the interdomain FMN to heme electron transfer in nitric oxide synthases

Nitric Oxide ◽  
2014 ◽  
Vol 42 ◽  
pp. 121
Author(s):  
Changjian Feng
2001 ◽  
Vol 276 (23) ◽  
pp. 20116-20124 ◽  
Author(s):  
Clinton R. Nishida ◽  
Paul R. Ortiz de Montellano

2014 ◽  
Vol 130 ◽  
pp. 130-140 ◽  
Author(s):  
Changjian Feng ◽  
Li Chen ◽  
Wenbing Li ◽  
Bradley O. Elmore ◽  
Wenhong Fan ◽  
...  

1998 ◽  
Vol 273 (10) ◽  
pp. 5566-5571 ◽  
Author(s):  
Clinton R. Nishida ◽  
Paul R. Ortiz de Montellano

2004 ◽  
Vol 71 ◽  
pp. 39-49 ◽  
Author(s):  
Dennis J. Stuehr ◽  
Chin-Chuan Wei ◽  
Jerome Santolini ◽  
Zhi- Qiang Wang ◽  
Mika Aoyagi ◽  
...  

NOSs (nitric oxide synthases) are flavohaem enzymes that function broadly in human health and disease. We are combining mutagenesis, crystallographic and rapid kinetic methods to understand their mechanism and regulation. The NOSs create a transient tetrahydrobiopterin radical within the enzyme to generate their free radical product (NO). Recent work is revealing how critically important this process is at all levels of catalysis. This article will synthesize four seemingly disparate but related aspects of NOS tetrahydrobiopterin radical formation: (i) how it enables productive O2 activation by providing an electron to the enzyme haem, (ii) what structural features help to regulate this electron transfer, (iii) how it enables NOS to synthesize NO from its diamagnetic substrate and (iv) how it allows NOS to release NO after each catalytic cycle instead of other nitorgen oxide-containing products.


Nitric Oxide ◽  
2017 ◽  
Vol 63 ◽  
pp. 61-67 ◽  
Author(s):  
Tobias M. Hedison ◽  
Sam Hay ◽  
Nigel S. Scrutton

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