Some properties of NAD-independent {alpha}-glycerophosphate dehydrogenase of yeast

NAD-independent, mitochondrial -glycerophosphate dehydrogenaseof baker's yeast, Saccharomyces cerevisiae, was liberated fromcells and its nature was examined. Hydrogen acceptors, pH optimaand reaction rates with substrate and hydrogen acceptor of theenzyme were determined. A naturally occurring phenolic pigmentextracted from yeast cells was also found to function as aneffective hydrogen acceptor for the enzyme. Addition of FMNor FAD to the -glycerophosphate oxidation system largely acceleratedenzymatic activity, whereas the enzyme system was strongly blockedby SH-reagents. This suggests that the SH-group functions atan essential site. Clear-cut inhibition by antimycin A of electrontransfer to cytochrome c suggests the intermediation of cytochromeb. (Received December 13, 1968; )