2005
CO 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