2004
The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain*
Konas D, Zhu K, Sharma M, Aulak K, Brudvig G, Stuehr D. The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain*. Journal Of Biological Chemistry 2004, 279: 35412-35425. PMID: 15180983, DOI: 10.1074/jbc.m400872200.Peer-Reviewed Original Research
1996
EPR Spectroscopic Characterization of Neuronal NO Synthase †
Galli C, MacArthur R, Abu-Soud H, Clark P, Stuehr D, Brudvig G. EPR Spectroscopic Characterization of Neuronal NO Synthase †. Biochemistry 1996, 35: 2804-2810. PMID: 8611587, DOI: 10.1021/bi9520444.Peer-Reviewed Original ResearchConceptsSpin-spin couplingElectron transferHeme ironElectron paramagnetic resonance spectroscopyEPR spectroscopic characterizationParamagnetic resonance spectroscopyOxygenase domainZero-field splitting parametersFirst coordination shellHeme redox centersNNOS oxygenase domainAir-stable semiquinoneSpectroscopic characterizationRedox centersReductase domainFlavin radicalsInterdomain electron transferFlavin semiquinoneCoordination shellResonance spectroscopyMicrowave power saturationSubstrates bindAnaerobic conditionsSubstrate bindingSemiquinone