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Inter-chromophore interactions in pigment-modified and dimer-less bacterial photosynthetic reaction centers

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Abstract

The magnitudes of inter-chromophore interactions in bacterial photosynthetic reaction centers are investigated by measuring absorption and Stark spectra of reaction centers in which monomeric chromophores are modified and in a novel triplet mutant which lacks the special pair. The circular dichroism spectrum of the triple mutant reaction center was also measured. Only small changes in the spectroscopic properties are observed, as has also been found for several types of reaction centers in which the absorption or chemical properties of a chromophore are altered by site-specific mutations. We conclude that the electronic absorption, circular dichroism and Stark features of the special pair and the monomeric chromophores in the reaction center are relatively insensitive to inter-chromophore interactions.

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References

  • Boxer SG (1993) Photosynthetic reaction center spectroscopy and electron transfer dynamics in applied electric fields. In: Deisenhofer J and Norris JR (eds) The Photosynthetic Reaction Center, pp 179–220. Academic Press, San Diego, CA

    Google Scholar 

  • Boxer SG, Franzen S, Lao K, Lockhart DJ, Stanley R, Steffen M, and Stocker JW (1992) Electric field effects on the quantum yields and kinetics of fluorescence and transient intermediates in bacterial reaction centers. In: Breton J and Verméglio A (eds) The Photosynthetic Bacterial Reaction Center II Structure, Spectroscopy, and Dynamics, pp 271–282. Plenum Publishing, New York

    Google Scholar 

  • Breton J (1985) Orientation of the chromophores in the reaction center of Rhodopseudomonas viridis. Comparison of the low-temperature linear dichroism spectra with a model derived from X-ray crystallography. Biochem Biophys Acta 810, 235–245

    Google Scholar 

  • Breton J (1988) Low temperature linear dichroism study of the orientation of the pigments in reduced and oxidized reaction centers of Rps. viridis and Rb. sphaeroides. In: Breton J and Verméglio A (eds) The Photosynthetic Bacterial Reaction Center Structure and Dynamics, pp 59–69, Plenum Press, New York

    Google Scholar 

  • Eberl U, Gilbert M, Keupp W, Langenbacher T, Siegl J, Sinning I, Ogrodnik A, Robles SJ, Breton J, Youvan DC, and Michel-Beyerle ME (1992) Fast internal conversion in bacteriochlorophyll dimers. In: Breton J and Verméglio A (eds) The Photosynthetic Bacterial Reaction Center II, pp 253–260. Plenum Press, New York

    Google Scholar 

  • Finkele U, Lauterwasser C, Struck A, Scheer H, and Zinth W (1992) Primary electron transfer kinetics in bacterial reaction centers with modified bacteriochlorophylls at the monomer sites BA;B. Proc Natl Acad Sci 89: 9514–9518

    Google Scholar 

  • Geskes C, Meyer M, Fischer M, Scheer H, and Heinze J (1995) Electrochemical investigation of modified photosynthetic pigments. J Phys Chem 99: 17669–17672.

    Google Scholar 

  • Goedheer JC (1966) Visible absorption and fluorescence of chlorophyll and its aggregates in solution. In: Vernon LP and Seely GR (eds) The Chlorophylls, pp 147–184. Academic Press, New York

    Google Scholar 

  • Goldsmith JO and Boxer SG (1996) Rapid isolation of bacterial photosynthetic reaction center with an engineered poly-histidine tag. Biochim Biophys Acta 1276: 171–175

    Google Scholar 

  • Goldsmith JO, King B, and Boxer SG (1996) Mg coordination by amino acid side chains is not required for assembly and function of the special pair in bacterial photosynthetic reaction centers. Biochemistry 35: 2421–2428

    Google Scholar 

  • Gottfried DS, Steffen MA, and Boxer SG (1991) Stark effect spectroscopy of carotenoids in photosynthetic antenna and reaction center complexes. Biochem Biophys Acta 1059: 76–90.

    Google Scholar 

  • Hammes SL, Mazzola L, Boxer SG, Gaul DF and Schenck CC (1990) Stark spectroscopy of the Rhodobacter sphaeroides reaction center heterodimer mutant. Proc Natl Acad Sci USA 87: 5682–5686

    Google Scholar 

  • Haran G, Wynne K, Moser CC, Dutton PL and Hochstrasser RM (1996) Level mixing and energy redistribution in bacterial photosynthetic reaction centers. J Phys Chem 100: 5562–5569

    Google Scholar 

  • Jackson JA, Lin S, Taguchi AKW, Williams JC, Allen JP and Woodbury NW (1997) Energy transfer in Rhodobacter sphaeroides reaction centers with the initial electron donor oxidized or missing. J Phys Chem B 101: 5747–5754

    Google Scholar 

  • Kirmaier C, Gaul D, DeBey R, Holten D and Schenck CC (1991) Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin. Science 251: 922–926

    Google Scholar 

  • Krawczyk S (1991) Electrochromism of chlorophyll a monomer and special pair dimer. Biochim Biophys Acta 1056: 64–70

    Google Scholar 

  • Laporte L, McDowell LM, Kirmaier C, Schenck CC and Holten D (1993) Insight into the factors controlling the rates of the deactivation processes that compete with charge separation in photosynthetic reaction centers. Chem Phys 176: 615–629

    Google Scholar 

  • Lee JK, Kiley PJ and Kaplan S (1989) Posttranscriptional control of puc operon expression of B800–850 light-harvesting complex-formation in Rb. sphaeroides. J Bacteriol 171: 3391–3405

    Google Scholar 

  • Lin X, Murchison HA, Nagarajan V, Parson WW, Allen JP and Williams JC (1994) Specific alterations of oxidation potentials of the electron donor in reaction centers from Rhodobacter sphaeroides. Proc Natl Acad Sci 91: 10265–10269

    Google Scholar 

  • Lockhart DJ and Boxer SG (1987) Magnitude and direction of the change in dipole-moment associated with excitation of the primary electron-donor in Rhodopseudomonas-sphaeroides reaction centers. Biochemistry 26: 664–668

    Google Scholar 

  • Meyer A and Scheer H (1995) Reaction centers of Rhodobacter sphaeroides R26 containing C-3 acetyl and vinyl bacteriochlorophyll at sites HA;B. Photosynth Res 44: 55–65

    Google Scholar 

  • Moore LJ and Boxer SG (1996) Cavity mutants involving residue L168 near the special pair dimer in reaction centers of Rb sphaeroides. Biophys J 70: MAMN3

    Google Scholar 

  • Moore LJ, Zhou H and Boxer SG. Manuscript in preparation

  • Murchison HA, Alden RG, Allen JP, Peloquin JM, Taguchi AKW, Woodbury NW and Williams JC (1993) Mutations designed to modify the environment of the primary electron donor of the reaction center from Rhodobacter sphaeroides: Phenylalanine to leucine at L167 and histidine to phenylalanine at L168. Biochemistry 32: 3498–3505

    Google Scholar 

  • Okamura M, Isaacson R and Feher G (1975) Primary acceptor in bacterial photosynthesis: Obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides. Proc Natl Acad Sci USA 72: 3491–3495

    Google Scholar 

  • Paddock ML, Rongney SH, Abresch EC, Feher G and Okamura MY (1988) Reaction center from 3 herbicide resistant mutant of Rhodobacter-sphaeroides 2.4.1: Sequence-analysis and preliminary characterization. Photosynth Res 17: 75–96

    Google Scholar 

  • Parson WW and Warshel A (1987) Spectroscopic properties of photosynthetic reaction centers. 2. Application of the theory to Rhodospeudomonas viridis. J Am Chem Soc 109: 6152–6163

    Google Scholar 

  • Parson W, Warshel A, Creighton S and Norris J (1988) Spectroscopic properties and electron transfer dynamics of reaction centers. In: Breton J and Verméglio A (eds) The Photosynthetic Reaction Center: Structure and Dynamics, pp 309–317. Plenum Press, New York

    Google Scholar 

  • Robles SJ, Breton J and Youvan DC (1990) Partial symmetrization of the photosynthetic reaction center. Science 248: 1402–1405

    Google Scholar 

  • Scheer H and Struck A (1993) Bacterial reaction centers with modified tetrapyrrole chromophores. In: Deisenhofer J and Norris JR (Eds) The Photosynthetic Reaction Center, pp 157–192. Academic Press, San Diego, CA

    Google Scholar 

  • Schenck C, Gaul D, Steffen M, Boxer SG, McDowell LM, Kirmaier C and Holten D. (1990) Site-directed mutations affecting primary photochemistry in reaction centers: Effects of dissymmetry in the special pair. In: Michel-Beyerle M-E (ed) Reaction Centers of the Photosynthetic Bacteria, pp 229–238. Spinger-Verlag, Berlin

    Google Scholar 

  • Schenck CC, Blankenship RE and Parson WW (1982) Radicalpair decay kinetics, triplet yields and delayed fluorescence from bacterial reaction centers. Biochim Biophys Acta 680: 44–59

    Google Scholar 

  • Scherer POJ and Fischer SF (1986) On the Stark effect for bacterial photosynthetic reaction centers. Chem Phys Lett 131: 153–159

    Google Scholar 

  • Scherer POJ and Fischer SF (1987) Model studies to low-temperature optical transition of photosynthetic reaction centers. II. Rhodobacter sphaeroides and Chloroflexus aurantiacus. Biochim Biophys Acta 891: 157–164

    Google Scholar 

  • Scherer POJ and Fischer SF (1991) Interpretation of optical reaction center spectra. In: Scheer H (ed) Chlorophylls, pp 1079–1093, CRC Press, Boca Raton, FL

    Google Scholar 

  • Scherz A and Parson WW (1984) Oligomers of bacteriochlorophyll and bacteriopheophytin with spectroscopic properties resembling those found in photosynthetic bacteria. Biochim Biophys Acta 766: 653

    Google Scholar 

  • Small GJ (1995) On the validity of the standard model for primary charge separation in the bacterial reaction center. Chem Phys 197: 239–257

    Google Scholar 

  • Stanley RJ, King B and Boxer SG (1996) Excited state energy transfer pathways in photosynthetic reaction centers. 1. Structural symmetry effects. J Phys Chem 100: 12052–12059

    Google Scholar 

  • Steffen MA (1995) Electrostatic interaction in photosynthetic reaction centers. PhD Thesis, Stanford

  • Struck A, Cmiel E, Katheder I, Schäfer W and Scheer H (1992) Bacteriochlorophylls modified at position C-3: long range intramolecular interaction with position C-13. Biochim Biophys Acta 1101: 321–328

    Google Scholar 

  • Struck A, Cmiel E, Katheder I and Scheer H (1990) Modified reaction centers from Rhodobacter sphaeroides R26. 2: Bacteriochlorophylls with modified C-3 substituents at sites BA and BB. FEBS Lett 268: 180–184

    Google Scholar 

  • Struck A, Müller A and Scheer H (1991) Modified bacterial reaction centers. 4. The borohydride treatment reinvestigated: comparison with selective exchange experiments at binding sites BA;B and HA;B. Biochim Biophys Acta 1060: 262–270

    Google Scholar 

  • Struck A and Scheer H (1990) Modified reaction centers from Rhodobacter sphaeroides R26. FEBS Lett 261: 385–388

    Google Scholar 

  • Thompson MA and Zerner MC (1991) A theoretical examination of the electronic structure and spectroscopy of the photosynthetic reaction center from Rps. viridis. J Am Chem Soc 113: 8210–8215

    Google Scholar 

  • van der Rest M and Gingras G (1974) The pigment complement of the photosynthetic reaction center isolated from Rhodospirillum rubrum. J Biol Chem 249: 6446

    Google Scholar 

  • Zhou H and Boxer SG (1997) Charge resonance effects on electronic absorption lineshapes: Applications to the heterodimer absorption of bacterial photosynthetic reaction centers. J Phys Chem B 101: 5759–5766

    Google Scholar 

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Moore, L.J., Boxer, S.G. Inter-chromophore interactions in pigment-modified and dimer-less bacterial photosynthetic reaction centers. Photosynthesis Research 55, 173–180 (1998). https://doi.org/10.1023/A:1005982002846

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