[Effect of molecular dynamics on the photoinduced electron transfer in eosin-myoglobin complex].
The temperature dependence of the rate constant of photoinduced electron transfer in the modified eosin-myoglobin complex by monitoring of the phosphorescence quenching of eosin is measured. The values of electron transfer rate constants are equal 10(2) + 10(3) s-1 in the temperature region 150-200 K. The kinetics of relaxation of the maximum of the time-resolved phosphorescence spectra of eosin on apomyoglobin is measured in the same temperature range. The solvation relaxation of the time-resolved phosphorescence spectra is nonexponential. The characteristic times of the solvation relaxation are given 10(-2) + 10(-4) s-1, that correlate with the time of electron transfer in this system. It was observed the "acceleration" of the relaxation rate of the time-resolved phosphorescence spectra of eosin in metmyoglobin due to nonequilibrium photoinduced electron transfer. The role of the matrix dynamics in photoinduced electron transfer in proteins is discussed.
Fogel'
V R
VR
Pastukhov
A V
AV
Psikha
B L
BL
Kotel'nikov
A I
AI
D000818:Animals; D004579:Electron Transport; D004801:Eosine Yellowish-(YS) / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D007700:Kinetics; D049449:Luminescence; D008786:Metmyoglobin / Q000737:chemistry*; D010777:Photochemistry; D013696:Temperature; D014907:Whales
D008786:Metmyoglobin; D006418:Heme; D004801:Eosine Yellowish-(YS)