Reaction mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Oxidation-reduction-active disulfides in the B1 subunit.
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Electron paramagnetic resonance spectra were recorded of three forms of Desulphovibrio gigas ferredoxin, FdI, FdI' and FdII. The g = 1.94 signal seen in dithionite-reduced samples is strong in FdI, weaker in FdI' and very small in FdII. The g = 2.02 signal in the oxidized proteins is weak in FdI and strongest in FdII. It is concluded that most of the 4Fe-4S centres in FdI change between states C- and C2-; FdI' contain both types of centre. There is no evidence that any particular centre can change reversibly between all three oxidation states. Circular dichroism spectra show differences between FdI and FdII even in the diamagnetic C2- state. The redox potentials of the iron-sulphur centres of the three oligomers (forms) are different. After formation of the apo-protein of FdII and reconstitution with iron and sulphide, the protein behaves more like FdI, showing a strong g = 1.94 signal in the reduced states.
Reduction capacity of the blood and its fractions was studied by potentiometry in 68 patients with the nephrotic syndrome. The type of renal injury was identified by kidney biopsy in all the patients. Control group consisted of 30 donors. Changes of blood reduction capacity were detected in all the patients with the nephrotic syndrome in comparison with the controls. A correlation could be traced between blood reduction capacity and functional compensation of the nephrotic syndrome. Disordered redox equilibrium was not associated in patients with the nephrotic syndrome with increased levels of lipid peroxidation products. The method used to assess reduction capacity is highly informative, rapid, and simple.
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