Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide

Hiroshi Okamoto; Arata Ichiyama; Osamu Hayaishi

doi:10.1016/0003-9861(67)90284-6

Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide

Hiroshi Okamoto, Arata Ichiyama, Osamu Hayaishi

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	110-114
Number of pages	5
Journal	Archives of Biochemistry and Biophysics
Volume	118
Issue number	1
DOIs	https://doi.org/10.1016/0003-9861(67)90284-6
Publication status	Published - 1967 Jan
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide",

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.",

author = "Hiroshi Okamoto and Arata Ichiyama and Osamu Hayaishi",

note = "Funding Information: 1 This investigation was supported in part by research grants from the National Institutes of Health (CA-04222 and AM-10333), the Jane Coffin Childs Memorial Fund for Medical Research, the Squibb Institute of Medical Research, and the Scientific Research Fund of the Ministry of Education of Japan.",

year = "1967",

month = jan,

doi = "10.1016/0003-9861(67)90284-6",

language = "English",

volume = "118",

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journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press Inc.",

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T1 - Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide

AU - Okamoto, Hiroshi

AU - Ichiyama, Arata

AU - Hayaishi, Osamu

N1 - Funding Information: 1 This investigation was supported in part by research grants from the National Institutes of Health (CA-04222 and AM-10333), the Jane Coffin Childs Memorial Fund for Medical Research, the Squibb Institute of Medical Research, and the Scientific Research Fund of the Ministry of Education of Japan.

PY - 1967/1

Y1 - 1967/1

N2 - 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.

AB - 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.

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