Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide

Hiroshi Okamoto, Arata Ichiyama, Osamu Hayaishi

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 languageEnglish
Pages (from-to)110-114
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume118
Issue number1
DOIs
Publication statusPublished - 1967 Jan
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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