2011
Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II
Pokhrel R, McConnell IL, Brudvig GW. Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II. Biochemistry 2011, 50: 2725-2734. PMID: 21366335, DOI: 10.1021/bi2000388.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexPhotosystem IICatalytic residuesChloride-binding siteRecent structural evidenceCyanobacterial photosystem IISalt bridgeEnzyme-substrate complexΑ-amylaseResidue crucialConformational shiftS-state cycleLys residuesCarboxylate residuesEnzyme turnoverChloride regulationResiduesD61Structural evidenceManganese clusterEnzymeBindingD1Potential mechanismsArg
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
Use of EPR Spectroscopy to Study Macromolecular Structure and Function
Biswas R, KÜhne H, Brudvig G, Gopalan V. Use of EPR Spectroscopy to Study Macromolecular Structure and Function. Science Progress 2001, 84: 45-68. PMID: 11382137, PMCID: PMC10367463, DOI: 10.3184/003685001783239050.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyProtein-nucleic acid complexesSpin-labeling reagentParamagnetic resonance spectroscopySpin labelsEPR spectroscopyAcid complexesBiological macromoleculesEPR spectraSite-specific substitutionMacromolecular structureResonance spectroscopyNucleic acidsSpectroscopyRecent applicationsStructural aspectsCommercial availabilityMacromoleculesCysteine residuesReagentsAdvent of techniquesStructure-function correlatesExperimental strategiesComplexesPowerful tool
1996
Effects of Dipole–Dipole Interactions on Microwave Progressive Power Saturation of Radicals in Proteins
Galli C, Innes J, Hirsh D, Brudvig G. Effects of Dipole–Dipole Interactions on Microwave Progressive Power Saturation of Radicals in Proteins. Journal Of Magnetic Resonance 1996, 110: 284-287. PMID: 8867444, DOI: 10.1006/jmrb.1996.0044.Peer-Reviewed Original Research