Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1316846 | Journal of Inorganic Biochemistry | 2016 | 9 Pages |
Abstract
During catalysis the nitric oxide (NO) synthases (NOSs) partition between a productive NO-releasing cycle and a futile NO dioxygenase cycle. We engineered NOS chimeras to manipulate the kinetic parameters that govern their catalytic cycling, so that they would function primarily as NO dioxygenases.127
Keywords
iNOSHeme reduction4-(2-hydroxyethyl)-1-piperazinepropanesulfonic acidFeIIINOSoxyH4BEPPSNEDnNOSeNOSNOSNADPHDTTFMNflavin adenine dinucleotideBSANω-hydroxy-l-argininel-argininebovine serum albuminArgelectron transferFADStopped-flowdithiothreitolSODinducible nitric oxide synthaseendothelial nitric oxide synthaseneuronal nitric oxide synthaseSuperoxide dismutaseCatalysisflavin mononucleotidelactate dehydrogenaseLDHkonNOHANitric oxidenitric oxide synthasenicotinamide adenine dinucleotide phosphateChimera
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Zhi-Qiang Wang, Mohammad Mahfuzul Haque, Katherine Binder, Manisha Sharma, Chin-Chuan Wei, Dennis J. Stuehr,