Glyceraldehyde-3-phosphate dehydrogenase-catalyzed chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals

J Biol Chem. 1980 Feb 10;255(3):874-6.


The chain oxidation of glyceraldehyde-3-phosphate dehydrogenase.NADH by perhydroxyl radicals and propagated by molecular oxygen was studied by the xanthine-xanthine oxidase system, 60Co gamma-ray, and pulse radiolysis. The chain length, amount of NADH oxidized per HO2 generated, increases with increasing acidity of the medium and reaches a value of 73 at pH 5.0. The rate constant for the oxidation of the glyceraldehyde-3-phosphate dehydrogenase.NADH complex by HO2 was estimated to be 2 X 10(7) M-1 S-1 at ambient temperatures (23-24 degrees C). Rate studies as a function of pH indicate that O2- is unreactive toward the glyceraldehyde-3-phosphate dehydrogenase.NADH complex. Other dehydrogenases (malate dehydrogenase, glutamate dehydrogenase, and isocitric dehydrogenase) studied showed no catalytic activity in the oxidation of NADH by HO2/O2-.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Free Radicals
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism*
  • Hydrogen-Ion Concentration
  • Isocitrate Dehydrogenase / metabolism
  • Kinetics
  • L-Lactate Dehydrogenase / metabolism
  • Liver / enzymology
  • Malate Dehydrogenase / metabolism
  • Muscles / enzymology
  • Myocardium / enzymology
  • NAD / metabolism*
  • Oxidation-Reduction
  • Rabbits
  • Swine


  • Free Radicals
  • NAD
  • L-Lactate Dehydrogenase
  • Malate Dehydrogenase
  • Isocitrate Dehydrogenase
  • Glyceraldehyde-3-Phosphate Dehydrogenases