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
Quantifying the Ion Selectivity of the Ca2+ Site in Photosystem II: Evidence for Direct Involvement of Ca2+ in O2 Formation †
Vrettos J, Stone D, Brudvig G. Quantifying the Ion Selectivity of the Ca2+ Site in Photosystem II: Evidence for Direct Involvement of Ca2+ in O2 Formation †. Biochemistry 2001, 40: 7937-7945. PMID: 11425322, DOI: 10.1021/bi010679z.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexTrivalent metal ionsMetal ionsPSII samplesPhotosystem IISubstrate water moleculesSmall metal ionsO2 evolutionSteady-state enzyme kineticsWater oxidationAqua ionsWater moleculesLewis acidO2 formationIonic radiusIon selectivityKcal/Monovalent ionsIonsExtrinsic polypeptidesFree energyEnzyme kineticsStructural cofactorSr2Activity measurementsEffects of tail‐like substituents on the binding of competitive inhibitors to the QB site of photosystem II
Reifler M, Szalai V, Peterson C, Brudvig G. Effects of tail‐like substituents on the binding of competitive inhibitors to the QB site of photosystem II. Journal Of Molecular Recognition 2001, 14: 157-165. PMID: 11391786, DOI: 10.1002/jmr.529.Peer-Reviewed Original ResearchConceptsQB siteAqueous phasePhotosystem IIBulk aqueous phaseCritical micelle concentrationTriazine-type herbicidesQuinone-binding sitePhenylurea moietyEffect of chargeAlkyl chainsHydrophobic tailSolvent conditionsMicelle concentrationPara positionPhenylurea compoundsS-triazineAlkylamino groupSubstituentsSmall libraryHydrophobic linkerMolecular rulerHydrophilic domainsNonspecific bindingChargeCompetitive inhibitor
1989
Chloride binding to photosystem II in the dark is in slow exchange
Shachar-Hill Y, Beck W, Brudvig G. Chloride binding to photosystem II in the dark is in slow exchange. FEBS Letters 1989, 254: 184-188. PMID: 2550276, DOI: 10.1016/0014-5793(89)81035-x.Peer-Reviewed Original Research
1980
Reactions of nitric oxide with cytochrome c oxidase.
Brudvig G, Stevens T, Chan S. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry 1980, 19: 5275-85. PMID: 6255988, DOI: 10.1021/bi00564a020.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesElectron Transport Complex IVNitric OxideOxidation-ReductionOxygenProtein BindingSpectrum Analysis
1979
Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region.
Bocian D, Lemley A, Petersen N, Brudvig G, Chan S. Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region. Biochemistry 1979, 18: 4396-402. PMID: 226125, DOI: 10.1021/bi00587a020.Peer-Reviewed Original Research