Oxidation of reduced nicotinamide hypoxanthine dinucleotide phosphate by intact rat liver mitochondria

Marc E Tischler, Ronald R. Fisher

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

1. 1. While intact rat liver mitochondria oxidize external NADPH at an extremely low rate (0.1-0.4 nmole per mg protein per min), reduced nicotinamide hypoxanthine dinucleotide phosphate (NHDPH) is relatively rapidly oxidized (12-13 nmoles per mg protein per min). 2. 2. After sonication, the rate of mitochondrial NHDPH oxidation is increased by 2-fold, and the NADPH oxidation rate is double that of NHDPH. 3. 3. NADPH and NHDPH oxidation is neither coupled to ATP synthesis nor inhibited by rotenone or CN-, but is inhibited under anaerobic conditions. These data indicate that, although molecular oxygen is the ultimate electron acceptor, the respiratory chain is not functional in the oxidation reaction. 4. 4. The NADPH oxidase activity resides in the submitochondrial particle fraction isolated from sonicated mitochondrial preparations. 5. 5. These results are interpreted to indicate the presence of an NADPH oxidase system in rat liver mitochondria which is bound to the inner surface of the inner membrane and independent of the respiratory chain. Further, it is concluded that the inner membrane may be significantly more permeable to NHDPH than to NADPH.

Original languageEnglish (US)
Pages (from-to)199-205
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume305
Issue number2
DOIs
StatePublished - May 30 1973
Externally publishedYes

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Mitochondria
Liver Mitochondrion
Liver
Rats
NADP
Phosphates
Oxidation
NADPH Oxidase
Electron Transport
Submitochondrial Particles
Membranes
Rotenone
Sonication
Molecular oxygen
Proteins
Adenosine Triphosphate
nicotinamide-hypoxanthine dinucleotide
Electrons
Oxygen

ASJC Scopus subject areas

  • Biophysics
  • Medicine(all)

Cite this

Oxidation of reduced nicotinamide hypoxanthine dinucleotide phosphate by intact rat liver mitochondria. / Tischler, Marc E; Fisher, Ronald R.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 305, No. 2, 30.05.1973, p. 199-205.

Research output: Contribution to journalArticle

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AB - 1. 1. While intact rat liver mitochondria oxidize external NADPH at an extremely low rate (0.1-0.4 nmole per mg protein per min), reduced nicotinamide hypoxanthine dinucleotide phosphate (NHDPH) is relatively rapidly oxidized (12-13 nmoles per mg protein per min). 2. 2. After sonication, the rate of mitochondrial NHDPH oxidation is increased by 2-fold, and the NADPH oxidation rate is double that of NHDPH. 3. 3. NADPH and NHDPH oxidation is neither coupled to ATP synthesis nor inhibited by rotenone or CN-, but is inhibited under anaerobic conditions. These data indicate that, although molecular oxygen is the ultimate electron acceptor, the respiratory chain is not functional in the oxidation reaction. 4. 4. The NADPH oxidase activity resides in the submitochondrial particle fraction isolated from sonicated mitochondrial preparations. 5. 5. These results are interpreted to indicate the presence of an NADPH oxidase system in rat liver mitochondria which is bound to the inner surface of the inner membrane and independent of the respiratory chain. Further, it is concluded that the inner membrane may be significantly more permeable to NHDPH than to NADPH.

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