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J. Biol. Chem., Vol. 256, Issue 11, 5577-5582, 06, 1981
T Ohnishi, TE King, JC Salerno, H Blum, JR Bowyer and T Maida
Thermodynamic parameters of succinate dehydrogenase flavin were determined
potentiometrically from the analysis of free radical signal levels as a
function of the oxidation-reduction potential. Midpoint redox potentials of
consecutive 1-electron transfer steps are -127 and - 31 mV at pH 7.0. This
corresponds to a stability constant of intermediate stability, 2.5 x
10(-2), which suggests flavin itself may be a converter from n = 2 to n = 1
electron transfer steps. The pK values of the free radical (FlH . in
equilibrium Fl . -) and the fully reduced form (FlH2 in equilibrium FlH-)
were estimated as 8.0 +/- 0.2 and 7.7 +/- 0.2, respectively. Succinate
dehydrogenase flavosemiquinone elicits an EPR spectrum at g = 2.00 with a
peak to peak width of 1.2 mT even in the protonated form, suggesting the
delocalization in the unpaired electron density. A close proximity of
succinate dehydrogenase flavin and iron-sulfur cluster S-1 was demonstrated
based on the enhancement of flavin spin relaxation by Center S-1.
Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase
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