Oxidation of reduced nicotinamide hypoxanthine dinucleotide by intact rat liver mitochondria

Marc E Tischler, Ronald R. Fisher

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

1. The rate of NADH oxidation catalyzed by intact rat liver mitochondria is greatly stimulated in the presence of oxidized nicotinamide hypoxanthine dinucleotide (NHD+). 2. Mitochondrial oxidation of external NHDH is from 20- to 40-fold more rapid than that of NADH, although these coenzymes are oxidized at similar rates by sonicated mitochondria. 3. NADH and NADPH inhibit, while NADP+ stimulates NHDH oxidation. 4. NHDH oxidation is inhibited by rotenone and CN-. 5. NHDH oxidation is coupled to the phosphorylation of ADP to ATP, yielding P:2e- ratios approaching 3. 6. These studies indicate that external NHDH is oxidized by the intramito-chondrial respiratory chain NADH dehydrogenase and that the inner mitochondrial membrane is significantly more permeable to NHDH than to NADH. Mammalian liver mitochondria have been reported to catalyze the enzymatic deamination of NAD(H) to NHD(H) [Buniatian, H. C. (1970) in Handbook of Neurochemistry (Lajtha, A., ed.), Vol. 3, pp. 399-411, Plenum Press, London and New York; Movcessian, S. G. and Manassian, R. F. (1967) in Problems of Brain Biochemistry, Vol. 3, pp. 53-66, Academic Press, Yerevan], suggesting a metabolic function for the deaminated analogue. It is concluded that this deamination reaction may be operative in a mechanism for the oxidation of cytoplasmic NADH by the respiratory chain.

Original languageEnglish (US)
Pages (from-to)39-49
Number of pages11
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume292
Issue number1
DOIs
StatePublished - Jan 18 1973
Externally publishedYes

Fingerprint

Mitochondria
Liver Mitochondrion
Liver
NAD
Rats
Oxidation
Deamination
Electron Transport
NADP
Neurochemistry
NADH Dehydrogenase
Rotenone
Biochemistry
Phosphorylation
Coenzymes
Mitochondrial Membranes
Adenosine Diphosphate
nicotinamide-hypoxanthine dinucleotide
Brain
Adenosine Triphosphate

ASJC Scopus subject areas

  • Biophysics
  • Medicine(all)

Cite this

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

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 292, No. 1, 18.01.1973, p. 39-49.

Research output: Contribution to journalArticle

@article{533b34ab51d94131998c937dd343aaf6,
title = "Oxidation of reduced nicotinamide hypoxanthine dinucleotide by intact rat liver mitochondria",
abstract = "1. The rate of NADH oxidation catalyzed by intact rat liver mitochondria is greatly stimulated in the presence of oxidized nicotinamide hypoxanthine dinucleotide (NHD+). 2. Mitochondrial oxidation of external NHDH is from 20- to 40-fold more rapid than that of NADH, although these coenzymes are oxidized at similar rates by sonicated mitochondria. 3. NADH and NADPH inhibit, while NADP+ stimulates NHDH oxidation. 4. NHDH oxidation is inhibited by rotenone and CN-. 5. NHDH oxidation is coupled to the phosphorylation of ADP to ATP, yielding P:2e- ratios approaching 3. 6. These studies indicate that external NHDH is oxidized by the intramito-chondrial respiratory chain NADH dehydrogenase and that the inner mitochondrial membrane is significantly more permeable to NHDH than to NADH. Mammalian liver mitochondria have been reported to catalyze the enzymatic deamination of NAD(H) to NHD(H) [Buniatian, H. C. (1970) in Handbook of Neurochemistry (Lajtha, A., ed.), Vol. 3, pp. 399-411, Plenum Press, London and New York; Movcessian, S. G. and Manassian, R. F. (1967) in Problems of Brain Biochemistry, Vol. 3, pp. 53-66, Academic Press, Yerevan], suggesting a metabolic function for the deaminated analogue. It is concluded that this deamination reaction may be operative in a mechanism for the oxidation of cytoplasmic NADH by the respiratory chain.",
author = "Tischler, {Marc E} and Fisher, {Ronald R.}",
year = "1973",
month = "1",
day = "18",
doi = "10.1016/0005-2728(73)90248-X",
language = "English (US)",
volume = "292",
pages = "39--49",
journal = "Biochimica et Biophysica Acta - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Oxidation of reduced nicotinamide hypoxanthine dinucleotide by intact rat liver mitochondria

AU - Tischler, Marc E

AU - Fisher, Ronald R.

PY - 1973/1/18

Y1 - 1973/1/18

N2 - 1. The rate of NADH oxidation catalyzed by intact rat liver mitochondria is greatly stimulated in the presence of oxidized nicotinamide hypoxanthine dinucleotide (NHD+). 2. Mitochondrial oxidation of external NHDH is from 20- to 40-fold more rapid than that of NADH, although these coenzymes are oxidized at similar rates by sonicated mitochondria. 3. NADH and NADPH inhibit, while NADP+ stimulates NHDH oxidation. 4. NHDH oxidation is inhibited by rotenone and CN-. 5. NHDH oxidation is coupled to the phosphorylation of ADP to ATP, yielding P:2e- ratios approaching 3. 6. These studies indicate that external NHDH is oxidized by the intramito-chondrial respiratory chain NADH dehydrogenase and that the inner mitochondrial membrane is significantly more permeable to NHDH than to NADH. Mammalian liver mitochondria have been reported to catalyze the enzymatic deamination of NAD(H) to NHD(H) [Buniatian, H. C. (1970) in Handbook of Neurochemistry (Lajtha, A., ed.), Vol. 3, pp. 399-411, Plenum Press, London and New York; Movcessian, S. G. and Manassian, R. F. (1967) in Problems of Brain Biochemistry, Vol. 3, pp. 53-66, Academic Press, Yerevan], suggesting a metabolic function for the deaminated analogue. It is concluded that this deamination reaction may be operative in a mechanism for the oxidation of cytoplasmic NADH by the respiratory chain.

AB - 1. The rate of NADH oxidation catalyzed by intact rat liver mitochondria is greatly stimulated in the presence of oxidized nicotinamide hypoxanthine dinucleotide (NHD+). 2. Mitochondrial oxidation of external NHDH is from 20- to 40-fold more rapid than that of NADH, although these coenzymes are oxidized at similar rates by sonicated mitochondria. 3. NADH and NADPH inhibit, while NADP+ stimulates NHDH oxidation. 4. NHDH oxidation is inhibited by rotenone and CN-. 5. NHDH oxidation is coupled to the phosphorylation of ADP to ATP, yielding P:2e- ratios approaching 3. 6. These studies indicate that external NHDH is oxidized by the intramito-chondrial respiratory chain NADH dehydrogenase and that the inner mitochondrial membrane is significantly more permeable to NHDH than to NADH. Mammalian liver mitochondria have been reported to catalyze the enzymatic deamination of NAD(H) to NHD(H) [Buniatian, H. C. (1970) in Handbook of Neurochemistry (Lajtha, A., ed.), Vol. 3, pp. 399-411, Plenum Press, London and New York; Movcessian, S. G. and Manassian, R. F. (1967) in Problems of Brain Biochemistry, Vol. 3, pp. 53-66, Academic Press, Yerevan], suggesting a metabolic function for the deaminated analogue. It is concluded that this deamination reaction may be operative in a mechanism for the oxidation of cytoplasmic NADH by the respiratory chain.

UR - http://www.scopus.com/inward/record.url?scp=0015928857&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015928857&partnerID=8YFLogxK

U2 - 10.1016/0005-2728(73)90248-X

DO - 10.1016/0005-2728(73)90248-X

M3 - Article

VL - 292

SP - 39

EP - 49

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 1

ER -