204
Views
21
CrossRef citations to date
0
Altmetric
Original Articles

Reconstitution of Photosynthetic Reaction Centers and Core Antenna-Reaction Center Complexes in Liposomes and Their Thermal Stability

, , , , , , , & show all
Pages 1130-1136 | Received 05 Jan 2005, Accepted 25 Feb 2005, Published online: 22 May 2014

  • 1) Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H., Structure of the protein subunits in the photosynthetic reaction center of Rhosopseudomonas viridis at 3 Å resolution. Nature, 318, 618–624 (1985).
  • 2) Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C., Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors. Proc. Natl. Acad. Sci. U.S.A., 84, 5730–5734 (1987).
  • 3) Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C., Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunit. Proc. Natl. Acad. Sci. U.S.A., 84, 6162–6166 (1987).
  • 4) Case, G. D., Parson, W. W., and Thornber, J. P., Photooxidation of cytochromes in reaction center preparations from Chromatium and Rhosopseudomonas viridis. Biochim. Biophys. Acta, 223, 122–128 (1970).
  • 5) Kennel, S. J., Bartsch, R. G., and Kamen, M. D., Observations on light-induced oxidation reactions in the electron transport system of Chromatium. Biophys. J., 12, 882–896 (1972).
  • 6) Madigan, M. T., A novel photosynthetic purple bacterium isolated from a Yellowstone hot spring. Science, 225, 313–315 (1984).
  • 7) Madigan, M. T., Chromatium tepidum sp. Nov., a thermophilic photosynthetic bacterium of the family Chromatiaceae. Int. J. Syst. Bacteriol., 36, 222–227 (1986).
  • 8) Nozawa, T., Trost, J. T., Fukada, T., Hatano, M., McManus, J. D., and Blankenship, R. E., Properties of the reaction center of the thermophilic purple photosynthetic bacterium Chromatium tepidum. Biochim. Biophys. Acta, 894, 468–476 (1987).
  • 9) Nozawa, T., and Madigan, M. T., Temperature and solvent effects on reaction centers from Chloroflexus aurantiacus and Chromatium tepidum. J. Biochem., 110, 588–594 (1991).
  • 10) Nogi, T., Insan, F., Kobayashi, M., Nozawa, T., and Miki, K., Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer. Proc. Natl. Acad. Soc. U.S.A., 97, 13561–13566 (2000).
  • 11) Insan, F., Mori, T., Nogi, T., Kobayashi, M., Miki, K., and Nozawa, T., Structure of the H subunit of the photosynthetic reaction center from the thermophilic purple sulfur bacterium, Thermochromatium tepidum. Implications for the specific binding of the lipid molecule to the membrane protein complex. Eur. J. Biochem., 268, 2652–2657 (2001).
  • 12) Nozawa, T., Fukada, T., Hatano, M., and Madigan, M. T., Organization of intra cytoplasmic membranes in a novel thermophilic purple photosynthetic bacterium as revealed by absorption, circular dichroism and emission spectra. Biochim. Biophys. Acta, 852, 191–197 (1986).
  • 13) Nozawa, T., Ohta, M., Hatano, M., Hayashi, H., and Shimada, K., Detergent effects on the reaction center-B890 complex of Chromatium vinosum and the mode of bacteriochlorophyll binding as revealed from circular dichroism and nuclear magnetic resonance spectroscopy. Biochim. Biophys. Acta, 850, 343–351 (1986).
  • 14) Wang, Z.-Y., Shimonaga, M., Kobayashi, M., and Nozawa, T., N-terminal methylation of the core light-harvesting complex in purple photosynthetic bacteria. FEBS Lett., 519, 164–168 (2002).
  • 15) Thornber, J. P., Photochemical reactions of purple bacteria as revealed by studies of three spectrally different. Carotenobacteriochlorophyll-protein complexes isolated from Chromatium, strain D. Biochemistry, 9, 2688–2698 (1970).
  • 16) Lin, L., and Thornber, J. P., Isolation and partial characterization of the photochemical reaction center of Chromatium vinosum (strain D). Photochem. Photobiol., 22, 37–40 (1975).
  • 17) Kobayashi, M., and Nozawa, T., Purification and crystallization of the reaction center from the thermophilic purple sulfur bacterium Chromatium tepidum. Bull. Chem. Soc. Jpn., 66, 3834–3836 (1993).
  • 18) Katayama, N., Kobayashi, M., Motojima, F., Inaka, K., Nozawa, T., and Miki, K., Preliminary X-ray crystallographic studies of photosynthetic reaction center from a thermophilic sulfur bacterium, Chromatium tepidum. FEBS Lett., 348, 158–160 (1994).
  • 19) Kobayashi, M., Takaya, A., Kanai, N., Ota, Y., Saito, T., Wang, Z.-Y., and Nozawa, T., Reconstitution and replacement of bacteriochlorophyll a molecules in photosynthetic reaction center. J. Biochem., 136, 363–369 (2004).
  • 20) Kagawa, Y., and Racker, E., Partial resolution of enzymes catalyzing oxidative phosphorylation. J. Biol. Chem., 246, 5477–5487 (1971).
  • 21) Scheer, H., Structure and occurrence of chlorophylls. In “Chlorophylls”, eds. Katz, J. J., Bowan, M. K., Michalski, T. J., and Worcester, D. L., CRC Press, Boca Raton, pp. 1–30 (1991).
  • 22) Scherz, A., and Parson, W. W., Oligomers of bacteriochlorophyll and bacteriopheophytins with spectroscopic properties resembling those found in photosynthetic bacteria. Biochim. Biophys. Acta, 766, 653–665 (1984).
  • 23) Scherz, A., and Rosenbach-Belkin, V., Comparative study of optical absorption and circular dichroism of bacteriochlorophyll oligomers in Triton X-100, the antenna pigment B850, and the primary donor P-860 of photosynthetic bacteria indicates that all are similar dimers of bacteriochlorophyll a. Proc. Natl. Acad. Sci. U.S.A., 86, 1505–1509 (1989).
  • 24) Michel, H., Epp, O., and Deisenhofer, J., Pigment-protein interactions in the photosynthetic reaction center from Rhodopseudomonas viridis. EMBO J., 5, 2445–2451 (1986).
  • 25) Ortega, J. M., and Mathis, P., Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis. Biochemistry, 32, 1141–1151 (1993).
  • 26) Ortega, J. M., Dohse, B., Oesterhelt, D., and Mathis, P., Low-temperature electron transfer from cytochrome to the special pair in Rhodopseudomonas viridis: Role of the L162 residue. Biophys. J., 74, 1135–1148 (1998).
  • 27) Fukushima, A., Matsuura, K., Shimada, K., and Satoh, T., Reaction center-B870 pigment protein complexes with bound cytochrome c-555 and c-551 from Rhodocyclus gelatinosus. Biochim. Biophys. Acta, 933, 399–405 (1988).
  • 28) Fathir, I., Ashikaga, M., Tanaka, K., Katano, T., Nirasawa, T., Kobayashi, M., Wang, Z.-Yu., and Nozawa, T., Biochemical and spectral characterization of the core light harvesting complex 1 (LH1) from the thermophilic purple sulfur bacterium Chromatium tepidum. Photosynth. Res., 58, 193–202 (1998).
  • 29) Sauer, K., and Austin, A., Bacteriochlorophyll-protein complexes from the light-harvesting antenna of photosynthetic bacteria. Biochemistry, 17, 2011–2019 (1978).
  • 30) Hayashi, H., Nozawa, T., Hatano, M., and Morita, S., Circular dichroism of bacteriochlorophyll a in light-harvesting bacteriochlorophyll-protein complexes from Chromatium vinosum. J. Biochem., 89, 1853–1861 (1981).
  • 31) Cogdell, R. J., Light-harvesting complexes in the purple photosynthetic bacteria. In “Photosynthesis III Photosynthetic Membrane and Light Harvesting Systems”, eds. Staehelin, L. A., and Arntzen, C. J., Springer-Verlag, Berlin, Germany, pp. 252–259 (1986).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.