Abstract
Many bacteria contain proton-translocating membrane-bound NADH-quinone oxidoreductases (NDH-1), which demonstrate significant genetic, spectral, and kinetic similarity with their mitochondrial counterparts. This review is devoted to the comparative aspects of the ironsulfur cluster composition of NDH-1 from the most well-studied bacterial systems to date.:Paracoccus denitrificans, Rhodobacter sphaeroides, Escherichia coli, andThermus thermophilus. These bacterial systems provide useful models for the study of coupling Site I and contain all the essential parts of the electron-transfer and proton-translocating machinery of their eukaryotic counterparts.
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Albracht, S. P. J., van Verseveld, H. W., Hagen, W. R., and Kalkman, M. L. (1980).Biochim. Biophys. Acta 593, 173–186.
Anraku, Y. (1988).Ann. Rev. Biochem. 57, 101–132.
Anraku, Y., and Gennis, R. B. (1987).Trends Biochem. Sci. 12, 262–266.
Arizmendi, J. M., Ruunswick, M. J., Skehel, J. M., and Walker, J. E. (1992a).FEBS Lett. 301, 237–242.
Arizmendi, J. M., Skehel, J. M., Ruunswick, M. J., Fearnley, I. M., and Walker, J. E. (1992b).FEBS Lett. 313, 80–84.
Baccarini-Melandri, A., Zannoni, D., and Melandri, B. A. (1973).Biochim. Biophys. Acta 314, 298–311.
Baugh, R. F., and King, T. E. (1972).Biochem Biophys. Res. Commun. 49, 1165–1173.
Beinert, H., and Albracht, S. P. J. (1982).Biochim. Biophys. Acta 683, 245–277.
Berks, B. C., and Ferguson, S. J. (1991).Biochem. Soc. Trans. 19, 581–588.
Blumberg, W. E., and Peisach, J. (1974).Arch. Biochem. Biophys. 162, 502–512.
Burbaev, D. Sh., Moroz, I. A., Kotlyar, A. B., Sled', V. D., and Vinogradov, A. D. (1989).FEBS Lett. 254, 47–51.
Calhoun, M. W., and Gennis, R. B. (1993).J. Bacteriol., in press.
Calhoun, M. W., Oden, K. L., Gennis, R. B., de Mattos, M. J. T., and Meijssel, O. M. (1993).J. Bacteriol., in press.
Cao, J., Hostler, J., Shapleigh, J., Revzin, A., and Ferguson-Miller, S. (1992).J. Biol. Chem. 267 24273–24278.
Cobley, J. G., Grossman, S., Singer, T. P., and Beinert, H. (1975).J. Biol. Chem. 250, 211–217.
Cotton, N. P. J., Lever, T. M., Nore, B. F., Jones, M. R., and Jackson, J. B. (1989).Eur. J. Biochem. 182, 593–603.
Cremona, T., and Kearney, E. J. (1964).J. Biol. Chem. 239, 2328–2334.
Dugad, L. B., La Mar, G. N., Banci, L., and Bertini, I. (1990).Biochemistry 29, 2263–2271.
Dupuis, A. (1992).FEBS Lett. 301, 215–218.
Dupuis, A., Skehel, J. M., and Walker, J. E. (1991).Biochem J. 224, 525–534.
Earley, F. G. P., Patel, S. D., Ragan, C. I., and Attardi, G. (1987).FEBS Lett. 219, 108–113.
Fee, J. A., Kuila, D., Mather, M. W., and Yoshida, T. (1986).Biochim. Biophys. Acta 853, 153–185.
Finel, M., Skehel, J. M., Albracht, S. P. J., Fearnley, I. M., and Walker, J. E. (1992).Biochemistry 31, 11425–11434.
Gennis, R. B., Casey, R. P., Azzi, A., and Ludwig, B. (1982).Eur. J. Biochem. 125, 189–195.
Gutman, M., Singer, T. P., and Beinert, H. (1972).Biochemistry 11, 556–562.
Hatefi, Y., Haavik, A. G., and Griffiths, D. (1962).J. Biol. Chem. 237, 1676–1680.
Hayashi, M., Miyoshi, T., Takashima, S., and Unemoto, T. (1989).Biochim. Biophys. Acta 977, 62–69.
Huang, P.-K. C., and Pharo, R. L. (1971).Biochim. Biophys. Acta 245, 240–244.
Ingledew, W. J., and Ohnishi, T. (1980).Biochem J. 186, 111–117.
Ingledew, W. J., and Pool, R. K. (1984).Microbiol. Rev. 84, 222–271.
Ingeldew, W. J., Reid, G. A., Poole, R. K., Blum, H., and Ohnishi, T. (1980).FEBS Lett. 111, 223–227.
Ise, W., Haiker, H., and Weiss, H. (1985).EMBO J. 2, 2075–2080.
John, P., and Whatley, F. R. (1975).Nature (London)254, 495–498.
Kagawa, Y. (1978).Biochim. Biophys. Acta 505, 45–93.
Kaniuga, Z., and Gardas, A. (1967).Biochim. Biophys. Acta 143, 647–649.
Kotlyar, A. B., Sled', V. D., Burbaev, D. Sh., Moroz, I. A., and Vinogradov, A. D. (1990).FEBS Lett. 264, 17–20.
Kroger, A., and Unden, G. (1985). InCoenzyme Q (Lenaz, G., ed.), Wiley, New York, pp. 285–300.
La Monica, R. F., and Marrs, B. L. (1976).Biochim. Biophys. Acta 423, 431–439.
Loundershausen, M., Leicht, W., Lieb, F., Moeschler, H., and Weiss, H. (1991).Pestic. Sci. 33, 427–438.
Ludwig, B., and Schatz, G. (1980).Proc. Natl. Acad. Sci. USA 77, 7732–7737.
Matsushita, K., Ohnishi, T., and Kaback, H. R. (1987).Biochemistry 26, 7732–7737.
Meinhardt, S. W., Kula, T., Yagi, T., Lillich, T., and Ohnishi, T. (1987).J. Biol. Chem. 262, 9147–9153.
Meinhardt, S. W., Matsushita, K., Kaback, H. R., and Ohnishi, T. (1989).Biochemistry 28, 2153–2160.
Meinhardt, S. W., Wang, D.-C., Hon-nami, K., Yagi, T., Oshima, T., and Ohnishi, T. (1990).J. Biol. Chem. 265, 1360–1368.
Ohnishi, T. (1973).Biochim. Biophys. Acta 301, 105–128.
Ohnishi, T. (1979). InMembrane Proteins in Energy Trunsduction (Capaldi, R. A., ed.), Marcel Dekker, New York, pp. 1–87.
Ohnishi, T., Leigh, J. S., Ragan, C. I., and Racker, E. (1974).Biochem. Biophys. Res. Commun. 56, 775–782.
Paech, C., Friend, A., and Singer, T. P. (1982).Biochem. J. 203, 477–481.
Pilkington, S. J., and Walker, J. E. (1989).Biochemistry 28, 3257–3264.
Pilkington, S. J., Arizmendi, J. M., Fearnley, I. M., Ruunswick, M. J., Skehel, J. M., and Walker, J. E. (1993).Biochem. Soc. Trans. 21, 26–31.
Ragan, C. I. (1978).Biochem J. 172, 539–547.
Ragan, C. I. (1990).Biochem. Soc. Trans. 18, 515–516.
Ragan, C. I., and Racker, E. (1973).J. Biol. Chem. 248, 6876–6884.
Ringler, R. L., Minakami, S., and Singer, T. P. (1963).J. Biol. Chem. 238, 801–810.
Runswick, M. J., Gennis, R. B., Fearnley, I. M., and Walker, J. E. (1989).Biochemistry 28, 9425–9459.
Schatz, C., and Racker, E. (1966).J. Biol. Chem. 241, 1429–1438.
Sled', V. D., Zinich, V. N., and Kotlyar, A. B. (1990).Biochemistry (USSR) 54, 1284–1288.
Sled', V. D., Rudnitzky, N., Hatefi, Y., and Ohnishi, T. (1993).Biophys. J. 64, A105.
Spiro, S., Roberts, R. E., and Guest, J. R. (1989).Mol. Microbiol. 3, 601–608.
Stouthamer, A. H. (1980).Trends Biochem. Sci. 6, 164–166.
Suzuki, H., and King, T. (1983).J. Biol. Chem. 258, 352–358.
Takamiya, K., Doi, M., and Okimatsu, H. (1982).Plant Cell. Physiol. 23, 987–997.
Trumpower, B. L. (1990).Microbiol. Rev. 52, 101–129.
Walker, J. E. (1992).Q. Rev. Biophys. 25, 253–324.
Weidner, U., and Weiss, H. (1992).Biochim. Biophys. Acta 1101, 151.
Weidner, U., Geier, S., Ptock, A., Friedrich, T., Leif, H., and Weiss, H. (1993).J. Mol. Biol., in press.
Weiss, H., Friedrich, Hofhaus, G., and Preis, D. (1991).Eur. J. Biochem. 197, 563–576.
Xu, X., Matsuno-Yagi, A., and Yagi, T. (1991a).Biochemistry 30, 6422–6428.
Xu, X., Matsuno-Yagi, A., and Yagi, T. (1991b).Biochemistry 30, 8678–8684.
Xu, X., Matsuno-Yagi, A., and Yagi, T. (1992a).Biochemistry 31, 6925–6932.
Xu, X., Matsuno-Yagi, A., and Yagi, T. (1992b).Arch. Biochem. Biophys. 296, 40–48.
Xu, X., Matsuno-Yagi, A., and Yagi, T. (1993).Biochemistry 32, 9688–981.
Yagi, T. (1986).Arch. Biochem. Biophys. 250, 302–311.
Yagi, T. (1991).J. Bioenerg. Biomembr. 23, 211–225.
Yagi, T. (1993).Biochim. Biophys. Acta 1141, 1–17.
Yagi, T., and Hatefi, Y. (1988).J. Biol. Chem. 263, 16150–16155.
Yagi, T., Hon-nami, K., and Ohnishi, T. (1988).Biochemistry 27, 2008–2013.
Yang, X., and Trumpower, B. L. (1986).J. Biol. Chem. 261, 12282–12289.
Yumoto, I., Wang, D.-C., Calhoun, M. W., Gennis, R. B., Friedrich, T., Weiss, H., and Ohnishi, T. (1992).Biochim. Biophys. Acta 1101, 152.
Yun, C.-H., Beci, R., Crofts, A. R., Kaplan, S., and Gennis, R. B. (1990).Eur. J. Biochem. 194, 399–411.
Zannoni, D., and Ingledew, W. J. (1983).FEMS Microbiol. Lett. 17, 331–334.
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Sled', V.D., Friedrich, T., Leif, H. et al. Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems. J Bioenerg Biomembr 25, 347–356 (1993). https://doi.org/10.1007/BF00762460
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DOI: https://doi.org/10.1007/BF00762460