Studies on succinic dehydrogenase. V. Isolation and properties of the dehydrogenase from baker's yeast

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Abstract

  • 1.

    1. The succinic dehydrogenase of baker's yeast has been solubilized and isolated from the particulate fraction of the cell wherein the enzyme is localized. The best preparations obtained were 65 % pure by ultracentrifugal analysis.

  • 2.

    2. The enzyme is an amber-brown protein, containing 4 atoms of iron and 1 mole of flavine per mole of protein. No method has been found to remove either the iron or the flavine without denaturation of the protein. The iron was readily liberated in the inorganic form by acid or thermal denaturation, but separation of the flavine from the protein required extensive proteolytic digestion of the latter. The flavine, set free in this manner, was not free FAD but, like that from the beef heart enzyme, appeared to be in bound form, possibly as peptide derivatives.

  • 3.

    3. The action of the enzyme is readily reversible. Inactivation on aging usually entailed a much greater loss of succinic dehydrogenase than of fumaric reductase activity.

  • 4.

    4. The following aspects of the action of the enzyme have been studied: effects of pH and temperature; specificity for electron carriers; inhibition by sulfhydryl reagents and iron complexors; kinetic constants for succinate, malonate, and fumarate; and turnover number.

  • 5.

    5. In most respects the yeast enzyme resembles closely its counterpart in beef heart mitochondria.

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  • Cited by (0)

    These studies were aided by a contract between the Office of Naval Research, Department of the Navy, and the Edsel B. Ford Institute for Medical Research, Nonr-1656(00), and by grants from the National Heart Institute, U. S. Public Health Service, and the American Heart Association. A preliminary report has appeared (1).

    2

    Established Investigator of the American Heart Association.

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