Abstract
Reaction centers (RC*) of purple bacteria are generally composed of three subunits designated H(igh), M(edium) and L(ow) according to their apparent molecular weigths on SDS PAGE. Four molecules of bacteriochlorophyll (Bchl) are bound to it, together with two bacteriopheophytins (Bphe), two quinones (Q) and one non-heme iron. The crystal structure of RC from the BChl b-containing purple photosynthetic bacterium, Rp. viridis (Deisenhofer et al, 1984) and from the Bchl a-containing Rb. sphaeroides (Chang et al., 1986; Allen et al., 1987) shows a C2 — symmetry axis which divides the reaction center into two very similar sets of pigments interacting mainly with the L and M-subunits, respectively. The reaction center is asymmetric, however, in functional terms. The primary charge separation takes place most probably from the special pair situated on the symmetry axis, via BpheL and QA situated on the L-(or ‘active’) branch of the complex, to QB on the M or ‘inactive’ branch (Deisenhofer et al., 1984; Vermeglio and Paillotin, 1982; Zinth et al., 1985).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Abbreviations
- RC:
-
reaction center
- Bchl:
-
bacteriochlorophyll
- Bphe:
-
bacteriopheophytin, the location of these pigments on the L- or M-branch of the RC is indicated by the respective subscript
- P870:
-
primary donor
- Chl:
-
chlorophyll
- Q:
-
quinone; subscript indicates the primary (A) or secondary acceptor (B) located on the L- and M-branch, respectively
- cd:
-
circular dichroism, ESR = electron spin resonance
- SDS-PAGE:
-
sodium dodecylsulfate polyacrylamide gel electrophoresis, LDAO = dimethyldodecylamineoxide, TX-100 = Triton X-100
- Rb.:
-
Rhodobacter
- Rp.:
-
Rhodopseudomonas, Rs. = Rhodospirillum, Cf. = Chloroflexus, Cr. = Chromatium.
References
Allen, J.P, G. Feher, T.O. Yeates, D.C. Rees, J. Deisenhofer, H. Michel und R. Huber, 1986, Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as detected by x-ray diffraction, Proc. Natl. Acad. sci. USA, 83:8589.
Angerhofer, A., J.U. von Schütz and H.C. Wolf, 1985, Fluorescence-ODMR of light harvesting pigments of photosynthetic bacteria, Z. Naturforsch. 40c:379.
Angerhofer, A., R.J. Cogdell and M.F. Hipkins, 1986 A spectral characterization of the light harvesting pigment-protein complexes from Rhodopseudomonas acidoprila. Biochim. Biophys. Acta 848:333.
Beese, D., Diplomarbeit, Universität München, 1984.
Beese, D., R. Steiner, H. Scheer, A. Angerhofer, B. Robert, and M. Lutz, 1987, Chemically modified photosynthetic bacterial reaction centers: Circular dichroism, Raman resonance, low temperature absorption, fluorescence and ODMR spectra and polypeptide composition of borohydride treated reaction centers from Rhodobacter sphaeroides R26, Photochem. Photobiol., in press.
Breton, J., J. Deprez, B. Tavitian, and E. Nabedryk, 1986, Spectroscopy, structure and dynamics in the reaction center of Rhodopseudomonas viridis, in: “Progress in Photosynthesis Research,” J. Biggins, ed., M. Nijhoff, Dordrecht, Vol. I., p. 387.
Chadwick, B.W., C. Zang, R.J. Cogdell, and H.A. Frank, 1987, The effects of lithium dodecyl sulfate and sodium borohydride on the absorption spectrum of the B800-850 light harvesting complex from Rhodopseudomonas acidophila 77 50, Biochim. Biophys. Acta, in press; see also contribution to this book.
Chang, C.-H., D. Tiede, J. Tang, V. Smith, J. Norris, and M. Schiffer, 1986, Structure of Rhodopseudomonas sphaeroides R-26 reaction centers, FEBS Lett., 205:82.
Clayton, R.K. and R.T. Wang, 1971, Photochemical Reaction Centers from Rhodopseudomonas sphaeroides., Methods Enzymol, 23:696.
Clayton, R.K. and B.J. Clayton, 1981, B850 pigment-protein complex of Rhodopseudomonas sphaeroides: extinction coefficients, circular dichroism, and the reversible binding of bacteriochlorophyll, Proc. Natl. Acad. Sci. USA 78:5583.
Crestfield, A.M., S. Moore and W.H. Stein, 1963, The preparation and enzymatic hydrolysis of reduced and S-Carboxymethylated proteins, J. Biol.Chem. 238:622.
Deisenhofer, J., O. Epp, K. Miki, R. Huber and H. Michel, 1984, X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and å model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis, J. Mol. Biol., 180:385.
Ditson, S.L., R.C. Davis and R.M. Pearlstein, 1984, Relative enrichment of P-870 in photosynthetic reaction centers treated with sodium Borohydride, Biochim. Biophys. Acta, 766:623.
Fischer, S.F. and P.O.J. Scherer, 1987, On the early charge separation and recombination processes in bacterial reaction centers. Chem. Phys., 115:151; see also contribution to this book.
Gottstein, J. and H. Scheer; 1983, Long-wavelength absorbing forms of bacteriochlorophyll a in solutions of Triton X-100, Proc. Natl. Acad. Sci. USA, 80:2231.
Holten, D., C. Kirmaier, and D. Levine, 1986, Picosecond studies of the kinetics and mechanisms of electron trasfer in bacterial reaction centers, in: “Progress in Photosynthesis Research,” J. Biggins, ed., M. Nijhoff, Dordrecht, Vol.1, p.169.
Hiyama, T., T. Watanabe, M. Kobayashi, and M. Nakazato, 1972, Interaction of chlorophyll a’ with the 65kDa subunit protein of photosystem I reaction center, FEBS Lett., 214:97.
Loach, P.A., M. Kung, and B. Hales, 1975, Characterization of the phototrap in photosynthetic bacteria, Ann. N.Y. Acad. Sci., 244:297.
Maroti, P., C. Kirmaier, C. Wraight, D. Holten and R.M. Pearlstein, 1985, Photochemistry and electron transfer in borohydride-treated photosynthetic reaction centers, Biochim. Biophys. Acta, 810:132.
Michel-Beyerle, M.E., M. Plato, J. Deisenhofer, H. Michel, M. Bixon, and J. Jortner, 1987, Unidirectionality of charge separation in reaction centers of photosynthetic bacteria. Biochim. Biophys. Acta, submitted for publication, see also contibution to this book.
Ogrodnik, A., H.W. Krüger, H. Orthuber, R. Haberkorn, M.E. Michel-Beyerle and H. Scheer, 1982, Recombination dynamics in bacterial photosynthetic reaction centers. Biophys. J., 39:91.
Parkes-Loach, P., J. Riccobono, and P. Loach, 1987, Preparation of subunits from the light-harvesting complex of Rhodospirilium rubrum, in: “Progress in Photosynthesis Research,” J. White, ed., M. Nijhoff, Dordrecht, Vol.II, p.25.
Parson, W.W., 1982, Photosynthetic bacterial reaction centers: Interactions among the bacteriochlorophylls and bacterio-pheophytins, Ann. Rev. Biophys. Bioeng., 11:57.
Plumley, F.G. and G.W. Schmidt, 1987, Reconstitution of chlorophyll a/b light harvesting complexes — Xanthophyll-dependent assembly and energy transfer, Proc. Natl. Acad. Sci. USA, 84:146.
Robert, B., M. Lutz and D.M. Tiede, 1985, Selective photochemical reduction of either of the two bacteriopheophytins in reaction centers of Rhodopseudomonas sphaerqides R-26. FEBS Lett., 183:326.
Robert, B., R. Steiner, Q. Zhou, H. Scheer and M. Lutz, 1986, Structures of antenna complexes and reaction centers from bacteriochlorophyll b-containing bacteria: Resonance raman studies, in: Progress in Photosynthesis Research, J. Biggins, ed., M. Nijhoff, Dordrecht, p.I.411.
Scheer, H., B. Paulke, J. Gottstein, 1985, Long-wavelength absorbing forms of bacteriochlorophyll a: II. Structural reguirements for formation in Triton X-100 micelles and in aqueous methanol and acetone, in: “Optical Properties and Structure of Tetrapyrroles”, G. Blauer, H. Sund, eds., de Gruyter, Berlin-New York, 1985, S.587.
Scherz, A. and W.W. Parson, 1984, Oligomers of bacteriochlorophyll and bacteriopheophytin with spectroscopic properties resembling those found in photosynthetic bacteria, Biochim.-Biophys. Acta., 766:653.
Scherz, A. and W.W. Parson, 1986, Interactions of the bacteriochlorophylls in antenna bacteriochlorophyll-protein complexes of photosynthetic bacteria, Photosynthesis Res., 9:21; see also contribution to this book.
Shuvalov, V.A., and L.N.M. Duysnes, 1986, Primary electron transfer reactions in modified reaction centers from Rhodopseudomonas sphaeroides. Proc. Natl. Acad. Sci. USA, 83:1690.
Shuvalov, V.A., A Ya. Shkuropatov, S.M. Kulakova, M.A. Ismailov and V.A. Shkuropatova, 1986, Photoreactions of bacteriopheophytins and bacteriochlorophylls in reaction centers of Rhodopseudomonas sphaeroides and Chloroflexus aurantiacus. Biochim. Biophys. Acta, 849:337.
Steiner, R., B. Kalumenos and H. Scheer, 1986, The photosynthetic apparatus of Ectothiorhodospira halochloris. 3. Effect of proteolytic digestion on the photoactivity, Z. Naturforsch., 41c:873.
Theiler, R., F. Suter, H. Zuber and R.J. Cogdell, 1984, A comparison of the primary structures of the two B 800-850-apoproteins from wild-type Rhodopseudomonas sphaeroides strain 2.4.1. and a carotenoidless mutant strain R 26.1, FEBS Lett., 175:231.
Vermeglio, A. and G. Paillotin, 1982, Structure of Rhodopseudomonas viridis reaction centers, absorption and photoselection at low-temperature, Biochim. Biophys. Acta, 681:32.
Wasielewski, M.R., 1986, Ultrafast electron and energy trasfer in reaction center and antenna proteins from photosynthetic bacteria, presented at the VIIth Int. Congr. Photosynthesis, Providence, 1986.
Wiemken, V. and R. Bachofen, 1984, Probing the smallest functional unit of the reaction center of Rhodospirillum rubrum G9 with proteinases, FEBS Lett., 166:155.
Zinth, W., M.C. Nuss, M.A. Franz, W. Kaiser, and H. Michel, 1983, in: Antennas and reaction centers of photosynthetic bacteria, M.E. Michel-Beyerle, ed., Springer, Berlin, p.286.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Springer Science+Business Media New York
About this chapter
Cite this chapter
Scheer, H., Beese, D., Steiner, R., Angerhofer, A. (1988). Reaction Centers of Purple Bacteria with Modified Chromophores. In: Breton, J., Verméglio, A. (eds) The Photosynthetic Bacterial Reaction Center. NATO ASI Series, vol 149. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0815-5_12
Download citation
DOI: https://doi.org/10.1007/978-1-4899-0815-5_12
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-0817-9
Online ISBN: 978-1-4899-0815-5
eBook Packages: Springer Book Archive