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
2001
Pulsed electron paramagnetic resonance methods for macromolecular structure determination
Lakshmi K, Brudvig G. Pulsed electron paramagnetic resonance methods for macromolecular structure determination. Current Opinion In Structural Biology 2001, 11: 523-531. PMID: 11785751, DOI: 10.1016/s0959-440x(00)00242-6.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance methodHigh-field EPRParamagnetic resonance methodMacromolecular structure determinationStructure elucidationEPR distance measurementsMacromolecular systemsStructure determinationStructure/function relationshipsRecent applicationsResonance methodMicrowave technologyFunction relationshipsEPRDeterminationRecent developmentsReview articlePowerful toolElucidation
1996
Characterization of the Reductase Domain of Rat Neuronal Nitric Oxide Synthase Generated in the Methylotrophic Yeast Pichia pastoris CALMODULIN RESPONSE IS COMPLETE WITHIN THE REDUCTASE DOMAIN ITSELF*
Gachhui R, Presta A, Bentley D, Abu-Soud H, McArthur R, Brudvig G, Ghosh D, Stuehr D. Characterization of the Reductase Domain of Rat Neuronal Nitric Oxide Synthase Generated in the Methylotrophic Yeast Pichia pastoris CALMODULIN RESPONSE IS COMPLETE WITHIN THE REDUCTASE DOMAIN ITSELF*. Journal Of Biological Chemistry 1996, 271: 20594-20602. PMID: 8702805, DOI: 10.1074/jbc.271.34.20594.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCalmodulinCalmodulin-Binding ProteinsDNA PrimersElectron Spin Resonance SpectroscopyFlavinsFlavoproteinsIsoenzymesMolecular Sequence DataNADH DehydrogenaseNeuronsNitric Oxide SynthaseOxidation-ReductionPichiaRatsRecombinant ProteinsSpectrometry, FluorescenceTryptophanConceptsElectron transferFlavin semiquinoneReductase domainNADPH-dependent flavin reductionArtificial electron acceptorsADP affinity chromatographyHeme-containing oxygenase domainCalmodulin responseNNOS reductase domainAnaerobic titrationFlavin reductionElectron acceptorNNOS reductaseFlavin-containing reductase domainReductase proteinSemiquinoneFlavinFlavin fluorescenceOxygenase domainAffinity chromatographyCytochrome c.Pure proteinCytochrome cTransferAcceptorEPR 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