Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1974 Jan;53(1):104–109. doi: 10.1104/pp.53.1.104

The Oxidation of Malate and Exogenous Reduced Nicotinamide Adenine Dinucleotide by Isolated Plant Mitochondria 1

D A Day a, J T Wiskich a
PMCID: PMC541342  PMID: 16658636

Abstract

Exogenous NADH oxidation by cauliflower (Brassica oleracea L.) bud mitochondria was sensitive to antimycin A and gave ADP/O ratios of 1.4 to 1.9. In intact mitochondria, NADH-cytochrome c reductase activity was only slightly inhibited by antimycin A. The antimycin-insensitive activity was associated with the outer membrane. Malate oxidation was sensitive to both rotenone and antimycin A and gave ADP/O values of 2.4 to 2.9. However in the presence of added NAD+, malate oxidation displayed similar properties to exogenous NADH oxidation. In both the presence and absence of added NAD+, malate oxidation was dependent on inorganic phosphate and inhibited by 2-n-butyl malonate.

Full text

PDF
108

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. CHANCE B., WILLIAMS G. R. The respiratory chain and oxidative phosphorylation. Adv Enzymol Relat Subj Biochem. 1956;17:65–134. doi: 10.1002/9780470122624.ch2. [DOI] [PubMed] [Google Scholar]
  2. Chappell J. B. Systems used for the transport of substrates into mitochondria. Br Med Bull. 1968 May;24(2):150–157. doi: 10.1093/oxfordjournals.bmb.a070618. [DOI] [PubMed] [Google Scholar]
  3. Coleman J. O.D., Palmer J. M. Role of Ca(2+) in the oxidation of exogenous NADH by plant mitochondria. FEBS Lett. 1971 Oct 1;17(2):203–208. doi: 10.1016/0014-5793(71)80148-5. [DOI] [PubMed] [Google Scholar]
  4. Coleman J. O., Palmer J. M. The oxidation of malate by isolated plant mitochondria. Eur J Biochem. 1972 Apr 24;26(4):499–509. doi: 10.1111/j.1432-1033.1972.tb01792.x. [DOI] [PubMed] [Google Scholar]
  5. Cunningham W. P. Oxidation of Externally Added NADH by Isolated Corn Root Mitochondria. Plant Physiol. 1964 Jul;39(4):699–703. doi: 10.1104/pp.39.4.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Douce R., Bonner W. D., Jr Oxalacetate control of Krebs cycle oxidations in purified plant mitochondria. Biochem Biophys Res Commun. 1972 May 12;47(3):619–624. doi: 10.1016/0006-291x(72)90923-0. [DOI] [PubMed] [Google Scholar]
  7. Douce R., Christensen E. L., Bonner W. D., Jr Preparation of intaintact plant mitochondria. Biochim Biophys Acta. 1972 Aug 17;275(2):148–160. doi: 10.1016/0005-2728(72)90035-7. [DOI] [PubMed] [Google Scholar]
  8. Douce R., Mannella C. A., Bonner W. D., Jr The external NADH dehydrogenases of intact plant mitochondria. Biochim Biophys Acta. 1973 Jan 18;292(1):105–116. doi: 10.1016/0005-2728(73)90255-7. [DOI] [PubMed] [Google Scholar]
  9. Ikuma H., Bonner W. D. Properties of Higher Plant Mitochondria. I. Isolation and Some Characteristics of Tightly-coupled Mitochondria from Dark-grown Mung Bean Hypocotyls. Plant Physiol. 1967 Jan;42(1):67–75. doi: 10.1104/pp.42.1.67. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Macrae A. R. Isolation and properties of a 'malic' enzyme from cauliflower bud mitochondria. Biochem J. 1971 May;122(4):495–501. doi: 10.1042/bj1220495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Miller R. J., Koeppe D. E. The effect of calcium and inhibitors on corn mitochondrial respiration. Plant Physiol. 1971 Jun;47(6):832–835. doi: 10.1104/pp.47.6.832. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Robinson B. H., Chappell J. B. The inhibition of malate, tricarboxylate and oxoglutarate entry into mitochondria by 2-n-butylmalonate. Biochem Biophys Res Commun. 1967 Jul 21;28(2):249–255. doi: 10.1016/0006-291x(67)90437-8. [DOI] [PubMed] [Google Scholar]
  14. Schnaitman C., Erwin V. G., Greenawalt J. W. The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol. 1967 Mar;32(3):719–735. doi: 10.1083/jcb.32.3.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sottocasa G. L., Kuylenstierna B., Ernster L., Bergstrand A. An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J Cell Biol. 1967 Feb;32(2):415–438. doi: 10.1083/jcb.32.2.415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Storey B. T., Bahr J. T. The Respiratory Chain of Plant Mitochondria: XIV. Ordering of Ubiquinone, Flavoproteins, and Cytochromes in the Respiratory Chain. Plant Physiol. 1972 Jul;50(1):95–102. doi: 10.1104/pp.50.1.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Storey B. T. The Respiratory Chain of Plant Mitochondria. III. Oxidation Rates of the Cytochromes c and b in Mung Bean Mitochondria Reduced With Succinate. Plant Physiol. 1969 Mar;44(3):413–421. doi: 10.1104/pp.44.3.413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Storey B. T. The Respiratory Chain of Plant Mitochondria: VI. Flavoprotein Components of the Respiratory Chain of Mung Bean Mitochondria. Plant Physiol. 1970 Jul;46(1):13–20. doi: 10.1104/pp.46.1.13. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wilson R. H., Hanson J. B. The effect of respiratory inhibitors on NADH, succinate and malate oxidation in corn mitochondria. Plant Physiol. 1969 Sep;44(9):1335–1341. doi: 10.1104/pp.44.9.1335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wojtczak L., Zaluska H. On the impermeability of the outer mitochondrial membrane to cytochrome c. I. Studies on whole mitochondria. Biochim Biophys Acta. 1969 Oct 14;193(1):64–72. doi: 10.1016/0005-2736(69)90059-5. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES