2025
Structure of a mutated photosystem II complex reveals changes to the hydrogen-bonding network that affect proton egress during O–O bond formation
Flesher D, Shin J, Debus R, Brudvig G. Structure of a mutated photosystem II complex reveals changes to the hydrogen-bonding network that affect proton egress during O–O bond formation. Journal Of Biological Chemistry 2025, 301: 108272. PMID: 39922494, PMCID: PMC11930075, DOI: 10.1016/j.jbc.2025.108272.Peer-Reviewed Original ResearchHydrogen bond networkProton egressWater moleculesO-O bond formationPhotosystem IIO-O bondStructure of photosystem IIHydrogen-bonded channelsWater-splitting enzymeRelease O<sub>2</sub> anProton egress pathwaysProton transferHydrogen bondsBond formationPhotosystem II complexSite-directed mutagenesisOxygen evolution rateReaction mechanismAmino groupsSide chainsCryo-EM structureCatalytic turnoverChloride ionsWater-protein interactionsD2 subunits
2024
Occupancy Analysis of Water Molecules inside Channels within 25 Å Radius of the Oxygen-Evolving Center of Photosystem II in Molecular Dynamics Simulations
Kaur D, Reiss K, Wang J, Batista V, Brudvig G, Gunner M. Occupancy Analysis of Water Molecules inside Channels within 25 Å Radius of the Oxygen-Evolving Center of Photosystem II in Molecular Dynamics Simulations. The Journal Of Physical Chemistry B 2024, 128: 2236-2248. PMID: 38377592, DOI: 10.1021/acs.jpcb.3c05367.Peer-Reviewed Original ResearchOxygen-evolving centerWater moleculesPhotosystem IIPositions of water moleculesAnalysis of water moleculesCatalyze water oxidationHydrogen bond networkOccupancy of water moleculesMolecular dynamics simulationsD1-D61Electron density mapsMolecular dynamics analysisProton transferWater oxidationCrystallographic dataIce latticeMD simulationsMolecular dynamicsStructural transitionDynamics simulationsSubstrate waterOxygen-evolvingRoom temperatureProtein residuesMolecules
2022
Glycerol binding at the narrow channel of photosystem II stabilizes the low-spin S2 state of the oxygen-evolving complex
Flesher DA, Liu J, Wiwczar JM, Reiss K, Yang KR, Wang J, Askerka M, Gisriel CJ, Batista VS, Brudvig GW. Glycerol binding at the narrow channel of photosystem II stabilizes the low-spin S2 state of the oxygen-evolving complex. Photosynthesis Research 2022, 152: 167-175. PMID: 35322325, PMCID: PMC9427693, DOI: 10.1007/s11120-022-00911-0.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexHydrogen bond networkS2 stateEPR signalPhotosystem II cyclesX-ray crystal structureRelative stabilityState EPR signalsD1-Asp61Water oxidationCatalytic intermediatesPhotochemical oxidationEPR spectraGlycerol moleculesCrystal structureCyanobacterial PSIIMultiline signalState SiPhotosystem IIOxidationRelative intensitiesComplexesEffect of glycerolExperimental conditionsStability
2007
Structural Analysis of Lac Repressor Bound to Allosteric Effectors
Daber R, Stayrook S, Rosenberg A, Lewis M. Structural Analysis of Lac Repressor Bound to Allosteric Effectors. Journal Of Molecular Biology 2007, 370: 609-619. PMID: 17543986, PMCID: PMC2715899, DOI: 10.1016/j.jmb.2007.04.028.Peer-Reviewed Original ResearchConceptsHydrogen bond networkHydrogen bondsExtensive hydrogen-bonding networkWater-mediated hydrogen bond networkSugar ringBond networkCrystal structureHydroxyl groupsAllosteric transitionEffector moleculesAnti-inducerSmall moleculesAtomic detailMoleculesStructural conformationC-terminal sub-domainBondsApo-repressorHydrogenHydroxylRepressor functionLac operonLac repressorN-terminalRepressor
2002
Proton-Transfer Dynamics in the Activation of Cytochrome P450eryF
Guallar V, Harris D, Batista V, Miller W. Proton-Transfer Dynamics in the Activation of Cytochrome P450eryF. Journal Of The American Chemical Society 2002, 124: 1430-1437. PMID: 11841312, DOI: 10.1021/ja016474v.Peer-Reviewed Original ResearchConceptsProton transfer eventsProton transfer dynamicsCytochrome P450eryFQuantum chemistry calculationsHydrogen bond networkMechanism of oxidationUltrafast proton transferMolecular dynamics simulationsProton transfer energy profileChemistry calculationsDistal oxygenOxyferrous stateBond networkProton transferEnergy profilesDynamics simulationsHeme groupEnzymatic efficacyP450eryFEnzymatic activationOxidationOxygen speciesReactionOxygenCytochrome P450
1999
A mechanistic and structural model for the formation and reactivity of a MnV[double bond, length half m-dash]O species in photosynthetic water oxidation
Limburg J, Szalai V, Brudvig G. A mechanistic and structural model for the formation and reactivity of a MnV[double bond, length half m-dash]O species in photosynthetic water oxidation. Dalton Transactions 1999, 0: 1353-1362. DOI: 10.1039/a807583b.Peer-Reviewed Original ResearchProtein complex photosystem IIPhotosynthetic water oxidationWater oxidationMn4 clusterModel complexesO bond-forming stepO bond-forming reactionsRedox-active tyrosine residueSubstrate water moleculesBond-forming reactionsO bond formationBond-forming stepHydrogen bond networkTetranuclear Mn clusterElectrophilic oxygen atomHydroxide ligandMnO speciesOrganic oxidationLength halfWater moleculesObserved reactivityBond formationNucleophilic attackOxygen atomsKey intermediate
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