The free NADH concentration is kept constant in plant mitochondria under different metabolic conditions

Plant Cell

Volumn 18, Issue 3, 2006, Pages 688-698

  Kasimova, Marina R ^a   Grigiene, Jurgita ^b   Krab, Klaas ^c   Hagedorn, Peter H ^a   Flyvbjerg, Henrik ^a   Andersen, Peter E ^a   Møller, Ian M ^d  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^b KAUNAS UNIVERSITY OF MEDICINE   (Lithuania)

^c VU UNIVERSITY AMSTERDAM   (Netherlands)

^d UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; METABOLISM; PLANT CELL CULTURE; PROTEINS;

ISOTHERMAL TITRATION CALORIMETRY; METABOLIC CONDITIONS; NADH; RESPIRATORY METABOLISM;

PLANTS (BOTANY);

METABOLISM; MITOCHONDRIA; PLANTS; PROTEINS;

SOLANUM TUBEROSUM;

LIGAND; MALIC ACID; MALIC ACID DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BIOLOGICAL MODEL; CYTOLOGY; HOMEOSTASIS; METABOLISM; MITOCHONDRION; OXIDATION REDUCTION REACTION; POTATO; SPECTROFLUOROMETRY;

HOMEOSTASIS; LIGANDS; MALATES; MITOCHONDRIA; MODELS, BIOLOGICAL; NAD; OXIDATION-REDUCTION; SOLANUM TUBEROSUM; SPECTROMETRY, FLUORESCENCE;

EID: 33646845908     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.039354     Document Type: Article

References (36)

1. Agius, S.C., Rasmusson, A.G., and Moøller, I.M. (2001). NAD(P) turnover in plant mitochondria. Aust. J. Plant Physiol. 28, 461-470.
2. Avi-Dor, Y., Olson, J.M., Doherty, M.D., and Kaplan, N.O. (1962). Fluorescence of pyridine nucleotides in mitochondria. J. Biol. Chem. 237, 2377-2383.
3. Blinova, K., Carroll, S., Bose, S., Smirnov, A.V., Harvey, J.J., Knutson, J.R., and Balaban, R.S. (2005). Distribution of mitochondrial NADH fluorescence lifetimes: Steady-state kinetics of matrix NADH interactions. Biochemistry 44, 2585-2594.
4. Bykova, N.V., Egsgaard, H., and Moøller, I.M. (2003). Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett. 540, 141-146.
5. +-linked substrates by pea leaf mitochondria. Physiol. Plant. 111, 448-456.
6. Ciotti, M.M., and Kaplan, N.O. (1957). Procedures for determination of pyridine nucleotides. Methods Enzymol. 3, 890-899.
7. Duysens, L.N.M., and Kronenberg, G.H.M. (1957). The fluorescence spectrum of the complex of reduced phosphopyridine nucleotide and alcohol dehydrogenase from yeast. Biochim. Biophys. Acta 26, 437-438.
8. French, S.A., Territo, P.R., and Balaban, R.S. (1998). Correction for inner filter effects in turbid samples: Fluorescence assays of mitochondrial NADH. Am. J. Physiol. 275, C900-C909.
9. Gafni, A., and Brand, L. (1976). Correction for inner filter effects in turbid samples: Fluorescence assays of mitochondrial NADH. Biochemistry 15, 3165-3171.
10. Hagedorn, P.H., Flyvbjerg, H., and Moøller, I.M. (2004). Modelling NADH turnover in plant mitochondria. Physiol. Plant. 120, 1-16.
11. Heineke, D., Riens, B., Grosse, H., Hoferichter, P., Peter, U., Flügge, U.-I., and Heldt, H.W. (1991). Redox transfer across the inner chloroplast envelope membrane. Plant Physiol. 95, 1131-1137.
12. Hirayama, K., Akashi, S., Furuya, M., and Fukuhara, K. (1990). Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS. Biochem. Biophys. Res. Commun. 173, 639-646.
13. Igamberdiev, A.D., and Gardeström, P. (2003). Regulation of NAD-and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves. Biochim. Biophys. Acta 1606, 117-125.
14. Krömer, S., and Heldt, H.W. (1991). Respiration of pea leaf mitochondria and redox transfer between the mitochondrial and extramitochondrial compartment. Biochim. Biophys. Acta 1057, 42-50.
15. Lakowics, J.R., Szmacinski, H., Nowaczyk, K., and Johnson, M.L. (1992). Fluorescence lifetime imaging of free and protein-bound NADH. Proc. Natl. Acad. Sci. USA 89, 1271-1275.
16. Langan, T.A. (1960). Changes in the fluorescence spectrum of reduced triphosphopyridine nucleotide on binding to isocitric dehydrogenase. Acta Chem. Scand. A 14, 936-938.
17. Moller, I.M. (2001). Plant mitochondria and oxidative stress. Electron transport, NADPH turnover and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 561-591.
18. Moøller, I.M., and Lin, W. (1986). Membrane-bound NAD(P)H dehydrogenses in higher plant cells. Annu. Rev. Plant Physiol. 37, 309-334.
19. Moøller, I.M., and Palmer, J.M. (1982). Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria. Physiol. Plant. 54, 267-274.
20. Moore, A.L., Dry, I.A., and Wiskich, J.T. (1988). Measurement of the redox state of the ubiquinone pool in plant mitochondria. FEBS Lett. 235, 76-80.
21. More, J.J. (1977). The Levenberg-Marquardt algorithm: Implementation and theory. In Numerical Analysis, Lecture Notes in Mathematics, Vol. 630. G. Watson, ed (Berlin: Springer-Verlag), pp. 105-116.
22. Neuburger, M., Day, D.A., and Douce, R. (1984). The regulation of malate oxidation in plant mitochondria by the redox state of endogenous pyridine nucleotides. Physiol. Veg. 22, 571-580.
23. Nicholls, D.G., and Ferguson, S.J. (2002). Bioenergetics 3. (Amsterdam: Academic Press).
24. Oliver, D.J., Neuburger, M., Bourgignon, J., and Douce, R. (1990). Glycine metabolism by plant mitochondria. Physiol, Plant. 80, 487-491.
25. +. Biochem. J. 208, 703-711.
26. Paul, R.J., and Schneckenburger, H. (1996). Oxygen concentration and the oxidation-reduction state of yeast: Determination of free/bound NADH and flavins by time-resolved spectroscopy. Naturwissenschaften 83, 32-35.
27. Petit, P.X., Sommarin, M., Pical, C., and Moøller, I.M. (1990). Modulation of endogenous protein phosphorylation in plant mitochondria by respiratory substrates. Physiol. Plant. 80, 493-499.
28. Putnam, F.W., ed (1975). The Plasma Proteins: Structure, Function, and Genetic Control. (New York: Academic Press), pp. 1, 141, 147.
29. Rasmusson, A.G., and Moøller, T.E. (1991). NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles. Physiol. Plant. 83, 357-365.
30. Rasmusson, A.G., Soole, K.L., and Elthon, T.E. (2004). Alternative NAD(P)H dehydrogenases of plant mitochondria. Annu. Rev. Plant Biol. 55, 23-39.
31. Scott, T.G., Spencer, R.D., Leonard, N.J., and Weber, G. (1970). Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models. J. Am. Chem. Soc. 92, 687-695.
32. Stocchi, V., Cucchiarini, L., Magnani, M., Chiarantini, L., Palma, P., and Cresentini, G. (1985). Simultaneous extraction and reversedphase high performance liquid Chromatographic determination of adenine and pyridine nucleotides in human blood cells. Anal. Biochem. 146, 118-124.
33. Struglics, A., Fredlund, K.M., Rasmusson, A.G., and Moøller, I.M. (1993). The presence of a short redox chain in the membrane of potato tuber peroxisomes and the association of malate dehydrogenase with the membrane. Physiol. Plant. 88, 19-28.
34. Subramanian, S., and Ross, P.D. (1978). Thermodynamics of binding of oxidized and reduced nicotinamide adenine dinucleotides, adenosine-5′- diphosphoribose, and 5′-iodosalicylate to dehydrogenases. Biochemistry 17, 2193-2197.
35. Wakita, M., Nishimura, G., and Tamura, M. (1995). Some characteristics of the fluorescence lifetime of reduced pyridine nucleotides in isolated mitochondria, isolated hepatocytes, and perfused rat liver in Situ. J. Biochem. (Tokyo) 118, 1151-1160.
36. Wiskich, J.T., Bryce, J.H., Day, D.A., and Dry, KB. (1990). Evidence for metabolic domains within the matrix compartment of pea leaf mitochondria. Plant Physiol. 93, 611-616.