Skip to main content
Log in

Regulation of Proton Flow and ATP Synthesis in Chloroplasts

  • Published:
Journal of Bioenergetics and Biomembranes Aims and scope Submit manuscript

Abstract

The chloroplast ATP synthase is strictly regulated so that it is very active in the light (rates of ATP synthesis can be higher than 5 μmol/min/mg protein), but virtually inactive in the dark. The subunits of the catalytic portion of the ATP synthase involved in activation, as well as the effects of nucleotides are discussed. The relation of activation to proton flux through the ATP synthase and to changes in the structure of enzyme induced by the proton electrochemical gradient are also presented. It is concluded that the γ and ε subunits of CF1 play key roles in both regulation of activity and proton translocation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

REFERENCES

  • Abrahams, J. P., Leslie, A. G., Lutter, R., and Walker, J. E. (1994). Nature (London) 370, 621-628.

    Google Scholar 

  • Avron, M., Krogmann, D. W., and Jagendorf, A. T. (1958). Biochim. Biophys. Acta 30, 144-153.

    Google Scholar 

  • Bar-Zvi, D., and Shavit, N. (1980). FEBS Lett. 118, 68-72.

    Google Scholar 

  • Bar-Zvi, D., and Shavit, N. (1982). J. Bioenerg. Biomembr. 14, 467-478.

    Google Scholar 

  • Bickelsandkoetter, S., and Strotmann, H. (1981). FEBS Lett. 125, 188-192.

    Google Scholar 

  • Boekema, E., van-Heel, M., and Graber, P. (1988). Progr. Clin. Biol. Res. 273, 75-80.

    Google Scholar 

  • Cross, R. L., and Duncan, T. M. (1996). J. Bioenerg. Biomembr. 28, 403-408.

    Google Scholar 

  • Cruz, J., Harfe, B., Radkowski, C., Dann, M., and McCarty, R. (1995). Plant Physiol. 109, 1379-1388.

    Google Scholar 

  • Cruz, J., Radkowski, C., and McCarty, R. (1997). Plant Physiol. 113, 1185-1192.

    Google Scholar 

  • Dann, M., S., and McCarty, R. E. (1992). Plant Physiol. 99, 153-160.

    Google Scholar 

  • Davenport, J. W., and McCarty, R. E. (1984). Biochim. Biophys. Acta 766, 363-374.

    Google Scholar 

  • Evron, Y., and Avron, M. (1990). Biochim. Biophys. Acta 1019, 115-120.

    Google Scholar 

  • Evron, Y., and McCarty, R. E. (2000). Plant Physiol. 124, 1-8.

    Google Scholar 

  • Evron, Y., and Pick, U. (1997). Plant Physiol. 115, 1549-1555.

    Google Scholar 

  • Fromme, P., Boekma, P., and Gräber, P. (1987a). Z. Naturforsch 42c, 1239-1245.

    Google Scholar 

  • Fromme, P., Gräber, P., and Salnikow, J. (1987b). FEBS Lett. 210, 27-30.

    Google Scholar 

  • Groth, G., and Junge, W. (1993). Biochemistry 32, 8103-8111.

    Google Scholar 

  • Higashida, M., and Mukohata, Y. (1976). J. Biochem. 80, 1177-1179.

    Google Scholar 

  • Hightower, K. E., and McCarty, R. E. (1996). Biochemistry 35, 4846-4851.

    Google Scholar 

  • Hisabori, T., Kato, Y., Motohashi, K., KrothPancic, P., Strotmann, H., and Amano, T. (1997). Eur. J. Biochem. 247, 1158-1165.

    Google Scholar 

  • Junesch, U., and Gräber, P. (1987). Biochim. Biophys. Acta 893, 275-288.

    Google Scholar 

  • Ketcham, S. R., Davenport, J. W., Warncke, K., and McCarty, R. E. (1984). J. Biol. Chem. 259, 7286-7293.

    Google Scholar 

  • Komatsu-Takaki, M. (1989). J. Biol. Chem. 264, 17750-12363.

    Google Scholar 

  • Komatsu-Takaki, M. (1996). Eur. J. Biochem. 236, 470-475.

    Google Scholar 

  • Magnusson, R. P., and McCarty, R. E. (1975). J. Biol. Chem. 250, 2593-2598.

    Google Scholar 

  • McCarty, R. E. (1997). Methods Enzymol. 278, 528-538.

    Google Scholar 

  • McCarty, R. E., and Fagan, J. (1973). Biochemistry 12, 1503-1507.

    Google Scholar 

  • McCarty, R. E., Fuhrman, J. S., and Tsuchiya, Y. (1971). Proc. Natl. Acad. Sci. USA 68, 2522-2526.

    Google Scholar 

  • Miki, J., Maeda, M., Mukohata, Y., and Futai, M. (1988). FEBS Lett. 232, 221-226.

    Google Scholar 

  • Mitchell, P. (1961). Nature (London) 191, 144-149.

    Google Scholar 

  • Moroney, J. V., and McCarty, R. E. (1982). J. Biol. Chem. 257, 5915-5920.

    Google Scholar 

  • Moroney, J. V., Fullmer, C. S., and McCarty, R. E. (1984). J. Biol. Chem. 259, 7281-7285.

    Google Scholar 

  • Portis, A. R. J., and McCarty, R. E. (1976). J. Biol. Chem. 251, 1610-1617.

    Google Scholar 

  • Portis, A. R. J., Magnusson, R. P., and McCarty, R. E. (1975). Biochem. Biophys. Res. Commun. 64, 877-884.

    Google Scholar 

  • Richter, M. L., and McCarty, R. E. (1987). J. Biol. Chem. 262, 15037-15040.

    Google Scholar 

  • Richter, M. L., Patrie, W. J., and McCarty, R. E. (1984). J. Biol. Chem. 259, 7371-7373.

    Google Scholar 

  • Richter, M. L., Hein, R., and Huchzermeyer, B. (2000). Biochim. Biophys. Acta 1458, 326-342.

    Google Scholar 

  • Schulenberg, B., Wellmer, F., Lill, H., Junge, W., and Engelbrecht, S. (1997). Eur. J. Biochem. 249, 134-141.

    Google Scholar 

  • Snyder, B., and Hammes, G. G. (1984). Biochemistry 23, 5787-5795.

    Google Scholar 

  • Soteropoulos, P., Suess, K. H., and McCarty, R. E. (1992). J. Biol. Chem. 267, 10348-10354.

    Google Scholar 

  • Soteropoulos, P., Ong, A., and McCarty, R. (1994). J. Biol. Chem. 269, 19810-19816.

    Google Scholar 

  • Wang, Z. Y., Freire, E., and McCarty, R. E. (1993). J. Biol. Chem. 268, 20785-20790.

    Google Scholar 

  • Weiss, M. A., and McCarty, R. E. (1977). J. Biol. Chem. 252, 8007-8012.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Evron, Y., Johnson, E.A. & McCarty, R.E. Regulation of Proton Flow and ATP Synthesis in Chloroplasts. J Bioenerg Biomembr 32, 501–506 (2000). https://doi.org/10.1023/A:1005669008974

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005669008974

Navigation