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• W1574914456 abstract "1. The kinetics of the reaction catalysed by succinate dehydrogenase (EC 1.3.99.1) have been studied. Double reciprocal plots (inverse of velocity against inverse of succinate concentration) at various concentrations of ferricyanide or phenazine methosulphate yield a series of straight lines converging in the third quadrant, when malonate is added. 2. Incubation with succinate of the enzyme prepared by the method of Keilin and King10 caused almost a doubling of the activity. 3. Both before and after activation with succinate, the catalytic-centre activity, measured at infinite substrate and acceptor concentrations, is the same with ferricyanide and phenazine methosulphate as acceptor. 4. At low concentrations ofphenazine methosulphate, the rate of the reaction is directly proportional to the acceptor concentration. 5. From the effect of succinate concentration on the intensity of optical absorption of the enzyme at 460 mμ, a dissociation constant of 110 μM was calculated. 6. The data support a mechanism in which the product of reaction between enzyme and substrate is oxidized by electron acceptor before dissociation of the product, fumarate, from the enzyme. No evidence could be obtained of an alternative pathway at 25° sufficiently rapid to make a significant contribution to the kinetics of the enzyme. 7. The main effect of activation is to increase the rate of intramolecular conversion of the enzyme-substrate complex, formed by reaction between enzyme and substrate, into a second complex which reacts with acceptor, and the reverse reaction. The reaction of this second complex with acceptor is also accelerated. 8. The catalytic centre activity of the activated enzyme, 130 sec−1 at 25°, agrees quite closely with that reported for particle-bound succinate dehydrogenase (about 200 sec−1 at 37°)." @default.
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• W1574914456 date "1969-04-01" @default.
• W1574914456 modified "2023-10-11" @default.
• W1574914456 title "Studies on succinate dehydrogenase" @default.
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• W1574914456 doi "https://doi.org/10.1016/0005-2744(69)90391-x" @default.
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