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 ligandsPhotolysisKineticsHemeMbCORapid timescale processes and the role of electronic surface coupling in the photolysis of diatomic ligands from heme proteins
Champion P, Rosca F, Ionascu D, Cao W, Ye X. Rapid timescale processes and the role of electronic surface coupling in the photolysis of diatomic ligands from heme proteins. Faraday Discussions 2004, 127: 123-135. PMID: 15471342, DOI: 10.1039/b316440c.Peer-Reviewed Original ResearchConceptsVibrational coherenceExcited state potential energy surfacesState potential energy surfaceLaser excitationSpin-forbidden naturePotential energy surfaceIron-histidine modeHeme protein myoglobinUltrafast time scaleIron spin stateRaman inactive modesFemtosecond laser excitationResonance Raman measurementsDiatomic ligandsEnergy surfaceGeminate recombinationUnpaired electronLigand dissociationSurface crossingsIron atomsUnphotolyzed stateVibrational frequenciesField interactionsExcited statesProtein myoglobin