A comparison between the effects of diethylether and urea on the electron transport system of R. rubrum was made.
Both reagents cause an increasing and complete inactivation of NADH oxidation with oxygen and cytochrome c as electron acceptors. The flavoprotein NADH dehydrogenase is only slightly affected. The oxidation of succinate (cytochrome c as electron acceptor) is inactivated only by much higher concentrations of either agent, succinate dehydrogenase being completely unaffected. Low concentrations of urea, in contrast to diethylether, stimulate succinate-cytochrome creductase. A preferential attack of both agents on the NADH → ubiquinone segment is suggested.
By treatment of the membranes with diethylether NADH dehydrogenase is transformed to a second, less active state. This form of the enzyme is characterized by a slower V max, a slightly increased k m(NADH), and an unchanged k m(electron acceptor). It cannot be reactivated.
Urea, like phosphate, causes a conformational change at the active site of succinate dehydrogenase as evidenced from an identical activation behaviour.
About 20% of the particulate activity of NADH dehydrogenase can be released from the membranes by treatment with urea. This activity apparently is identical with that solubilized by deoxycholate.
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Boll, M. Structure and function of electron transport systems. Archiv. Mikrobiol. 76, 174–182 (1971). https://doi.org/10.1007/BF00411791
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