NAD+ Reduction by Ferrocyanide on the Surface of Bovine Heart Mitochondrion

drial outer membrane oxidizes exogenous NADH. The elec-trons contained in this exogenous nucleotide are transferred at the beginning with the support of NADH-cytochrome b5 reductase2 (EC 1.6.2.2, abbreviated to NCBR in this report) to cytochrome b5. This cytochrome constructing mitochon-drial outer membrane gives its electron to cytochrome c which is an electron shuttle2 between inner and outer mem-branes. Palmer wrote in one of his writings that all reactions catalysed by enzymes are reversible to some degree.3 In par-allel with Palmer, Nicholls described in his Bioenergetics that much of the respiratory chain is reversible.4 The bovine-heart mitochondria, presenting excellent oxidative activity for exogenous NADH,5 were made to reduce NAD+ for its reduced counterpart production with the support of an ferro-cyanide, an artificial reductant, in this study. Demonstratin