THE PYRUVIC DEHYDROGENASE SYSTEM OF CLOSTRIDIUM PASTEURIANUM

Authors:
  • DWD. W. S. Westlake
    D. W. S. Westlake
  • ASA. L. Shug
    A. L. Shug
  • PWP. W. Wilson
    P. W. Wilson

Abstract
The pyruvic dehydrogenase system of Clostridium pasteurianum has been shown to catalyze a multistep reaction. Spectrophotometric experiments with aged and dialyzed preparations have implicated flavin, the hydrogenase system, and iron in this reaction. Molybdenum, which is not required for the normal action of the hydrogenase system, is needed in some form for the reduction of one-electron acceptors. The carbon monoxide combining component of this system is not of the hemochromogen type and must be in the reduced state before combining with carbon monoxide. A scheme is presented for the liberation of hydrogen from pyruvate by cell-free extracts in the presence of methyl viologen.

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