The kinetics of the succinoxidase |
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Authors: | G S Eadie F Bernheim |
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Institution: | (1) Department of Physiology and Pharmacology, Duke University School of Medicine, Durham, North Carolina |
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Abstract: | Rate equations for the enzymatic oxidation of succinic acid are derived on the assumption that when a single molecule of substrate
combines with an enzyme molecule, it can do so with either one or two sites on the enzyme, and that oxidation occurs only
in the second case. In addition it is assumed that the product of the reaction, fumaric acid, combines reversibly with the
enzyme. With certain enzyme preparations the data fitted such an equation satisfactorily. In others the rate was that of a
first-order reaction, but addition of cytochrome changed it to the former type. It was concluded that the transfer of hydrogen
to oxygen was a first-order reaction and dominated the whole rate when enzyme preparations were used which had been washed
relatively free of cytochrome. When the limiting factor was succino-dehydrogenase the rates followed the new equation. Criteria
for recognizing noncompetitive inhibition are given, and inhibition by di-tertiary butyl peroxide was shown to be of this
type. |
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Keywords: | |
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