Abstract
Reduced α-nicotinamide adenine dinucleotide (α-NADH) is oxidized at about one fifth of the rate of reduced β-nicotinamide adenine dinucleotide by rat liver mitochondria that have been treated with a hypotonic medium. Essentially no oxidation is observed with intact mitochondria. Oxidation is almost completely inhibited by 1 mm cyanide, but is insensitive to 1 μm antimycin A, 1 μm rotenone, and 2 mm anytal. Furthermore, enzyme activities have been detected that catalyze the transfer of electrons from α-NADH to cytochrome c and to 2,6-dichlorophenolindophenol and are seemingly localized in the microsomal and soluble fractions, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 110-114 |
| Number of pages | 5 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 118 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1967 Jan |
| Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
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Cite this
Okamoto, H., Ichiyama, A., & Hayaishi, O. (1967). Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide. Archives of Biochemistry and Biophysics, 118(1), 110-114. https://doi.org/10.1016/0003-9861(67)90284-6