2015
Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)
Wong EV, Cao W, Vörös J, Merchant M, Modis Y, Hackney DD, Montpetit B, De La Cruz EM. Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). Journal Of Molecular Biology 2015, 428: 492-508. PMID: 26730886, PMCID: PMC4744555, DOI: 10.1016/j.jmb.2015.12.018.Peer-Reviewed Original Research
2013
Quantitative full time course analysis of nonlinear enzyme cycling kinetics
Cao W, De La Cruz EM. Quantitative full time course analysis of nonlinear enzyme cycling kinetics. Scientific Reports 2013, 3: 2658. PMID: 24029878, PMCID: PMC3772379, DOI: 10.1038/srep02658.Peer-Reviewed Original ResearchConceptsKinetic time coursesProduct inhibitionSteady-state enzyme kinetic parametersReaction schemeEnzymology approachReaction productsReversible bindingEnzyme kinetic parametersProduct releasePractical general methodKinetic parametersEnzyme inhibitionGeneral methodProductsEnzyme systemEnzymatic parameters
2012
Plus‐end directed myosins accelerate actin filament sliding by single‐headed myosin VI
Ramamurthy B, Cao W, De La Cruz EM, Mooseker MS. Plus‐end directed myosins accelerate actin filament sliding by single‐headed myosin VI. Cytoskeleton 2012, 69: 59-69. PMID: 22213699, PMCID: PMC3327287, DOI: 10.1002/cm.21002.Peer-Reviewed Original Research
2011
Kinetic Analysis of Autotaxin Reveals Substrate-specific Catalytic Pathways and a Mechanism for Lysophosphatidic Acid Distribution*
Saunders LP, Cao W, Chang WC, Albright RA, Braddock DT, De La Cruz EM. Kinetic Analysis of Autotaxin Reveals Substrate-specific Catalytic Pathways and a Mechanism for Lysophosphatidic Acid Distribution*. Journal Of Biological Chemistry 2011, 286: 30130-30141. PMID: 21719699, PMCID: PMC3191052, DOI: 10.1074/jbc.m111.246884.Peer-Reviewed Original ResearchConceptsLysophosphatidic acidSecreted lysophospholipase DThr-210Synthase cycleVivo substrateSubstrate bindingQuantitative physiological modelsSignaling cascadesPosition 210LPA signalingCatalytic threonineFluorescent lipidLysophospholipase DCancer metastasisSlow catalysisCatalytic pathwayDiazol-4PathwayAutotaxinProduct releaseBindsLPA synthesisFS-3Acid distributionBioactive form
2007
The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpA
Henn A, Cao W, Hackney DD, De La Cruz EM. The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpA. Journal Of Molecular Biology 2007, 377: 193-205. PMID: 18237742, PMCID: PMC2359651, DOI: 10.1016/j.jmb.2007.12.046.Peer-Reviewed Original ResearchFluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
Zhang H, Cao W, Zakharova E, Konigsberg W, De La Cruz EM. Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates. Nucleic Acids Research 2007, 35: 6052-6062. PMID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.Peer-Reviewed Original ResearchConceptsHydroxyl groupsNucleotidyl transfer reactionMinimal kinetic schemeConformational changesDetectable fluorescence changeChemical quenchTransfer reactionsDependent fluorescence enhancementFluorescence enhancementFluorescence quenchingFluorescent probeRapid conformational changesTemplate complexN-positionRate constantsFluorescence changesRapid fluorescenceTernary complexKinetic schemeComplexesTemplating baseDependent conformational changesDp/TTemplateFluorescence
2006
Energetics and Kinetics of Cooperative Cofilin–Actin Filament Interactions
Cao W, Goodarzi JP, De La Cruz EM. Energetics and Kinetics of Cooperative Cofilin–Actin Filament Interactions. Journal Of Molecular Biology 2006, 361: 257-267. PMID: 16843490, DOI: 10.1016/j.jmb.2006.06.019.Peer-Reviewed Original Research
2005
Thermodynamics of Nucleotide Binding to Actomyosin V and VI: A Positive Heat Capacity Change Accompanies Strong ADP Binding †
Robblee JP, Cao W, Henn A, Hannemann DE, De La Cruz EM. Thermodynamics of Nucleotide Binding to Actomyosin V and VI: A Positive Heat Capacity Change Accompanies Strong ADP Binding †. Biochemistry 2005, 44: 10238-10249. PMID: 16042401, DOI: 10.1021/bi050232g.Peer-Reviewed Original ResearchMagnesium, ADP, and Actin Binding Linkage of Myosin V: Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States †
Hannemann DE, Cao W, Olivares AO, Robblee JP, De La Cruz EM. Magnesium, ADP, and Actin Binding Linkage of Myosin V: Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States †. Biochemistry 2005, 44: 8826-8840. PMID: 15952789, DOI: 10.1021/bi0473509.Peer-Reviewed Original ResearchCO Rebinding to Protoheme: Investigations of the Proximal and Distal Contributions to the Geminate Rebinding Barrier
Ye X, Yu A, Georgiev G, Gruia F, Ionascu D, Cao W, Sage J, Champion P. CO Rebinding to Protoheme: Investigations of the Proximal and Distal Contributions to the Geminate Rebinding Barrier. Journal Of The American Chemical Society 2005, 127: 5854-5861. PMID: 15839683, PMCID: PMC2768272, DOI: 10.1021/ja042365f.Peer-Reviewed Original ResearchConceptsProximal imidazole ligandRebinding barrierImidazole ligandsCetyltrimethylammonium bromideMicelles of cetyltrimethylammonium bromideAbsence of imidazoleDifferent solvent conditionsFree energy barrierCO rebinding ratesLigation changesGeminate amplitudeCO recombinationEnthalpic barrierDistal pocketRebinding kineticsCO rebindingHistidine ligationEnergy barrierEntropic contributionsEnthalpic contributionSolvent conditionsLigation statesSolvent viscosityWeak ligandsLigand
2004
Investigations of Photolysis and Rebinding Kinetics in Myoglobin Using Proximal Ligand Replacements †
Cao W, Ye X, Sjodin T, Christian J, Demidov A, Berezhna S, Wang W, Barrick D, Sage J, Champion P. Investigations of Photolysis and Rebinding Kinetics in Myoglobin Using Proximal Ligand Replacements †. Biochemistry 2004, 43: 11109-11117. PMID: 15323570, DOI: 10.1021/bi049077g.Peer-Reviewed Original ResearchConceptsCO rebinding kineticsRebinding kineticsDiatomic ligandsRaman spectraH93G myoglobinLigand vibrational modesLaser flash photolysisResonance Raman spectraBind exogenous ligandsWild-type MbCOCO rebinding ratesTime-resolved Raman spectroscopyProximal ligandFlash photolysisGeminate phaseVibrational modesProximal linkageLigandRebinding rateKinetic resultsExogenous ligandsPhotolysisKineticsHemeMbCOProximal and Distal Influences on Ligand Binding Kinetics in Microperoxidase and Heme Model Compounds †
Cao W, Ye X, Georgiev G, Berezhna S, Sjodin T, Demidov A, Wang W, Sage J, Champion P. Proximal and Distal Influences on Ligand Binding Kinetics in Microperoxidase and Heme Model Compounds †. Biochemistry 2004, 43: 7017-7027. PMID: 15170339, DOI: 10.1021/bi0497291.Peer-Reviewed Original ResearchConceptsRebinding kineticsTime-resolved IR measurementsCO docking sitesLaser flash photolysisLigand rebinding kineticsTime-resolved Raman spectraCO rebinding kineticsTime-resolved Raman spectroscopyFe-protoporphyrin IXFlash photolysisGeminate rebindingLigand binding kineticsHeme complexNative myoglobinRaman spectraIR measurementsVibrational modesMicelle-encapsulatedDilution conditionsMicroperoxidaseLigandBinding kineticsKineticsEnergetic significanceConcentration samples
2001
Water Penetration and Binding to Ferric Myoglobin †
Cao W, Christian J, Champion P, Rosca F, Sage J. Water Penetration and Binding to Ferric Myoglobin †. Biochemistry 2001, 40: 5728-5737. PMID: 11341838, DOI: 10.1021/bi010067e.Peer-Reviewed Original ResearchConceptsH2O bindingHeme pocketHydrogen bondsHis-64Heme ironFlash photolysis investigationsPhotodissociation of NOFerric heme proteinsH2O ligandsWater moleculesNO photolysisHorse heart metmyoglobinHeme proteinsCO escapeBound waterRebinding rateSmall moleculesH2OPhotolysisDissociation constantBondsHydrogenHemeMoleculesPhysiological NO concentrations