Free energy dependence of the rate of long-range electron transfer in proteins. Reorganization energy in ruthenium-modified myoglobin

1988 ◽  
Vol 110 (2) ◽  
pp. 599-600 ◽  
Author(s):  
Jennifer L. Karas ◽  
Charles M. Lieber ◽  
Harry B. Gray
1989 ◽  
Vol 111 (4) ◽  
pp. 1315-1319 ◽  
Author(s):  
Kurt V. Mikkelsen ◽  
Jens Ulstrup ◽  
Merab G. Zakaraya

Science ◽  
1990 ◽  
Vol 247 (4946) ◽  
pp. 1069-1071 ◽  
Author(s):  
L. S. Fox ◽  
M. Kozik ◽  
J. R. Winkler ◽  
H. B. Gray

2017 ◽  
Vol 6 (6) ◽  
pp. 267-275
Author(s):  
Maurice Ohaekeleihem Iwunze

Steady-state fluorescence spectroscopy was used to study the interaction of riboflavin with nicotine in a bicontinuous microemulsion system made up of 42.11:13.70:21.34:22.85 % w/w of water: oil: surfactant: cosurfactant. The surfactant used is cetyltrimethylammonium bromide (CTAB), the oil is tetradecane and the cosurfactant is 1-pentanol. It is observed that the interaction of riboflavin and nicotine in the prepared microemulsion lead to the quenching of riboflavin fluorescence. The bimolecular quenching rate constant, kq, of riboflavin by nicotine was observed as 4.15 x 109 M-1 s -1 with an efficiency of 56 %. The mechanism of the reaction is proposed to be diffusion limited in an activated electron transfer reaction in a solvent separated (outer-sphere) scheme. The electron transfer rate constant, kET, was calculated as 5.89 x 109 s -1 with an activation rate constant, ka, of 9.52 x 109 s -1 . The calculated solvent reorganization energy, λs, of the reaction was 1.09 eV, the free energy of interaction, ΔGo , is -2.9 eV and the free energy of activation, ΔG*, was calculated as 0.75 eV.


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