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 Research
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 ligandsPhotolysisKineticsHemeMbCO
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