Abstract
There are multiple routes of NAD(P)H oxidation associated with the inner membrane of plant mitochondria. These are the phosphorylating NADH dehydrogenase, otherwise known as Complex I, and at least four other nonphosphorylating NAD(P)H dehydrogenases. Complex I has been isolated from beetroot, broad bean, and potato mitochondria. It has at least 32 polypeptides associated with it, contains FMN as its prosthetic group, and the purified enzyme is sensitive to inhibition by rotenone. In terms of subunit complexity it appears similar to the mammalian and fungal enzymes. Some polypeptides display antigenic similarity to subunits fromNeurospora crassa but little cross-reactivity to antisera raised against some beef heart complex I subunits. Plant complex I contains eight mitochondrial encoded subunits with the remainder being nuclear-encoded. Two of these mitochondrial-encoded subunits, nad7 and nad9, show homology to corresponding nuclear-encoded subunits inNeurospora crassa (49 and 30 kDa, respectively) and beef heart CI (49 and 31 kDa, respectively), suggesting a marked difference between the assembly of CI from plants and the fungal and mammalian enzymes. As well as complex I, plant mitochondria contain several type-II NAD(P)H dehydrogenases which mediate rotenone-insensitive oxidation of cytosolic and matrix NADH. We have isolated three of these dehydrogenases from beetroot mitochondria which are similar to enzymes isolated from potato mitochondria. Two of these enzymes are single polypeptides (32 and 55 kDa) and appear similar to those found in maize mitochondria, which have been localized to the outside of the inner membrane. The third enzyme appears to be a dimer comprised of two identical 43-kDa subunits. It is this enzyme that we believe contributes to rotenone-insensitive oxidation of matrix NADH. In addition to this type-II dehydrogenases, several observations suggest the presence of a smaller form of CI present in plant mitochondria which is insensitive to rotenone inhibition. We propose that this represents the peripheral arm of CI in plant mitochondria and may participate in nonphosphorylating matrix NADH oxidation.
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Arron, G. P., and Edwards, G. E. (1980).Plant Physiol. 65, 591–594.
Barrera, C. R., Namihira, G., Hamilton, C., Munk, P. Eley, M. H., Linn, T. C., and Reed, L. J. (1972).Arch. Biochem. Biophys. 148, 343–358.
Brunton, C. J., and Palmer, J. M. (1973).Eur. J. Biochem. 39, 283–291.
Bryce, J. H., Azcon-Bieto, J., Wiskich, J. T., and Day, D. A. (1990).Physiol. Plant. 78, 105–111.
Büschges, R., Bahrenberg, G., Zimmermann, M., and Wolf, K. (1994).Yeast 10, 475–479.
Carlenor, E., Persson, B., Glaser, E., Andersson, B., and Rydstrom, J. (1988).Plant Physiol. 88, 303–308.
Chauveau, M., and Lance, C. (1990).Plant Physiol. 95, 934–942.
Cook, N. D., and Cammack, R. (1984).Eur. J. Biochem. 141, 573–577.
Cook, N. D., and Cammack, R. (1985).Biochim. Biophys. Acta 827, 30–35.
Cottingham, I. R., and Moore, A. L. (1984).Biochem. J. 224, 171–179.
Crowder, S. E., and Ragan, C. I. (1977).Biochem. J. 165, 295–301.
Day, D. A., Rayner, J. R., and Wiskich, J. T. (1976).Plant Physiol. 58, 38–42.
Day, D. A., Whelan, J., Millar, A. H., Siedow, J. N., and Wiskich, J. T. (1995).Aust. J. Plant. Physiol. 22, in press.
Earley, F. G. p., Patel, S. D., Ragan, C. I., and Attardi, G. (1987).FEBS Lett. 219, 108–113.
Ernster, L. (1987).Chem. Scr. 27A, 1–13.
Fredlund, K. M., Rasmusson, A. G., and Møller, I. M. (1991).Plant Physiol. 97, 99–103.
Friedrich, T., Hofhaus, G., Ise, W., Nehls, U., Schmitz, B., and Weiss, H. (1989).Eur. J. Biochem. 180, 173–180.
Friedrich, T., Strohdeicher, M., Hofhaus, G., Preis, D., Sahm, H., and Weiss, H. (1990).FEBS Lett. 265, 37–40.
Friedrich, T., Weidner, U., Nehls, U., Fecke, W., Schneider, R., and Weiss, H. (1993).J. Bioenerg. Biomembr. 25, 331–337.
Friedrich, T., Van Heek, P., Leif, H., Ohnishi, T., Forche, E., Knuze, B., Jansen, R., Trowitzsch-Kienast, W., Hofle, G., Reichenbach, H. and Weiss, H. (1994).Eur. J. Biochem. 219, 691–698.
Gäbler, L., Herz, U., Liddell, A., Leaver, C. J., Schröder, W., Brennicke, A., and Grohmann, L. (1994).Mol. Gen. Genet. 244, 33–40.
Hatefi, Y., Haavik, A. G., and Griffiths, D. E. (1962).J. Biol. Chem. 237, 1676–1680.
Herz, U., Schröder, W., Liddell, A., Leaver, C. J., Brennicke, A., and Grohmann, L. (1994).J. Biol. Chem. 269, 2263–2269.
Hofhaus, G., and Attardi, G. (1993).EMBO J. 12, 3043–3048.
Klein, R. R., and Burke, J. J. (1984).Plant Physiol. 76, 436–441.
Knudten, A. F., Thelen, J. J., Leuthy, M. H., and Elthon, T. E. (1994).Plant Physiol. 106, 1115–1122.
Koeppe, D. E., and Miller, R. J. (1972).Plant Physiol. 49, 353–357.
Kromer, S., Hianning, I., and Heldt, H. W. (1992). InMolecular, Biochemical and Physiological Aspects of Plant Respiration. (Lambers, H., and Van Der Plas, L. H. W., eds.), SPB Academic Publishing, The Hague, pp. 167–176.
Kubo, T., Mikami, T., and Kinoshita, T. (1993).Mol. Gen. Genet. 241, 479–482.
Lamattina, L., Gonzalez, D., Gualberto, J., and Grienenberger, J. M. (1993).Eur. J. Biochem. 217, 831–838.
Leif, H., Weidner, U., Breger, A., and Spehr, V. (1993).Biochem. Soc. Trans. 21, 998–1001.
Leterme, S., and Boutry, M. (1993).Plant Physiol. 102, 435–443.
Leuthy, M. H., Hayes, M. K., and Elthon, T. E. (1991).Plant Physiol. 97, 1317–1322.
Leuthy, M. H., Knudten, A. F., and Elthon, T. E. (1992). InMolecular, Biochemical, and Physiological Aspects of Plant Respiration. (Lambers, H., and Van Der Plas, L. H. W., eds.), SPB Academic Publishing, The Hague, pp. 29–36.
Leuthy, M. H., Thelen, J. J., Knudten, A. F., and Elthon, T. E. (1995).Plant Physiol. 107, 443–450.
Menz, R. I., Griffith, M., Day, D. A., and Wiskich, J. T. (1992).Eur. J. Biochem. 208, 481–485.
Møller, I. M., and Lin, W. (1986).Annu. Rev. Plant. Physiol. 37, 309–334.
Møller, I. M., and Palmer, J. M. (1981).Physiol. Plant. 53, 413–420.
Møller, I. M., and Palmer, J. M. (1982).Physiol. Plant. 54, 267–274.
Møller, I. M., Rasmusson, A. G., and Fredlund, K. M. (1993).J. Bioenerg. Biomembr. 25, 377–384.
Nash, D., and Wiskich, J. T. (1983).Plant Physiol. 71, 627–634.
Nehls, U., Friedrich, T., Schmeide, A., Ohnishi, T., and Weiss, H. (1992).J. Mol. Biol. 227, 1032–1042.
Oda, K., Yamato, K., Ohta, E., Nakamura, Y., Takemura, M., Nozato, N., Akashi, K., Kanegae, T., Kohchi, T., and Ohyama, K. (1992).J. Mol. Biol. 223, 1–7.
Rasmusson, A. G., and Møller, I. M. (1991a).Physiol. Plant. 83, 357–356.
Rasmusson, A. G., and Møller, I. M. (1991b).Eur. J. Biochem. 202, 617–623.
Rasmusson, A. G., Fredlund, K. M., and Møller, I. M. (1993).Biochim. Biophys. Acta 1141, 107–110.
Rasmusson, A. G., Mendel-Hartvig, J., Møller, I. M., and Wiskich, J. T. (1994).Physiol. Plant. 90, 607–615.
Ravanel, P., Tissuut, M., and Douce, R. (1986).Plant Physiol. 80, 500–504.
Rayner, J. R., and Wiskich, J. T. (1983).Aust. J. Plant. Physiol. 10, 55–63.
Rugolo, M., and Zannoni, D. (1992).Plant Physiol. 99, 1037–1043.
Rychter, A. M., Chauveau, M., Bomsel, J.-L., and Lance, C. (1992).Physiol. Plant. 84, 80–86.
Schmidt, M., Friedrich, T., Wallrath, J., Ohnishi, T., and Weiss, H. (1992).FEBS Lett. 313, 8–11.
Schulte, U., Fecke, W., Krull, C., Nehls, U., Schmiede, A., Schneider, R., Ohnishi, T., and Weiss, H. (1994).Biochim. Biophys. Acta 1187, 121–124.
Soole, K. L. (1989). Unpublished PhD Thesis, The University of Adelaide, South Australia.
Soole, K. L., Dry, I. B., James, A. T., and Wiskich, J. T. (1990).Physiol. Plant. 80, 75–82.
Soole, K. L., Dry, I. B., and Wiskich, J. T. (1992).Plant Physiol. 98, 588–594.
Tuschen, G., Scakmann, U., Nehls, U., Haiker, H., Buse, G., and Weiss, H. (1990).J. Mol. Biol. 213, 845–857.
Walker, J. E. (1992).Q. Rev. Biophys. 25, 253–324.
Weiss, H., Friedrich, T., Hofhaus, G., and Preis, D. (1991).Eur. J. Biochem. 197, 563–576.
Wiskich, J. T., and Bonner, W. D. (1963).Plant. Physiol. 38, 594–604.
Wiskich, J. T., and Menz, R. I. (1993). InPlant Mitochondria (Brennicke, A., and Kuck, U., eds.), VCH, Weinheim, Germany, pp. 261–274.
Yagi, T. (1993).Biochim. Biophys. Acta 1141, 1–17.
Zambrano, M., and Kolter, R. (1993).J. Bacteriol. 175, 5642–5647.
Zottini, M., Mandolino, G., and Zannoni, D. (1993).Plant Physiol. 102, 579–585.
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Soole, K.L., Menz, R.I. Functional molecular aspects of the NADH dehydrogenases of plant mitochondria. J Bioenerg Biomembr 27, 397–406 (1995). https://doi.org/10.1007/BF02110002
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DOI: https://doi.org/10.1007/BF02110002