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. 2001 Mar;80(3):1487–1497. doi: 10.1016/S0006-3495(01)76121-8

Effect of high pressure on the photochemical reaction center from Rhodobacter sphaeroides R26.1.

A Gall 1, A Ellervee 1, M C Bellissent-Funel 1, B Robert 1, A Freiberg 1
PMCID: PMC1301340  PMID: 11222309

Abstract

High-pressure studies on the photochemical reaction center from the photosynthetic bacterium Rhodobacter sphaeroides, strain R26.1, shows that, up to 0.6 GPa, this carotenoid-less membrane protein does not loose its three-dimensional structure at room temperature. However, as evidenced by Fourier-transform preresonance Raman and electronic absorption spectra, between the atmospheric pressure and 0.2 GPa, the structure of the bacterial reaction center experiences a number of local reorganizations in the binding site of the primary electron donor. Above that value, the apparent compressibility of this membrane protein is inhomogeneous, being most noticeable in proximity to the bacteriopheophytin molecules. In this elevated pressure range, no more structural reorganization of the primary electron donor binding site can be observed. However, its electronic structure becomes dramatically perturbed, and the oscillator strength of its Q(y) electronic transition drops by nearly one order of magnitude. This effect is likely due to very small, pressure-induced changes in its dimeric structure.

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Selected References

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  1. Cogdell R. J., Frank H. A. How carotenoids function in photosynthetic bacteria. Biochim Biophys Acta. 1987;895(2):63–79. doi: 10.1016/s0304-4173(87)80008-3. [DOI] [PubMed] [Google Scholar]
  2. Deisenhofer J., Epp O., Miki K., Huber R., Michel H. X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol. 1984 Dec 5;180(2):385–398. doi: 10.1016/s0022-2836(84)80011-x. [DOI] [PubMed] [Google Scholar]
  3. Feher G. Some chemical and physical properties of a bacterial reaction center particle and its primary photochemical reactants. Photochem Photobiol. 1971 Sep;14(3):373–387. doi: 10.1111/j.1751-1097.1971.tb06180.x. [DOI] [PubMed] [Google Scholar]
  4. Fowler G. J., Sockalingum G. D., Robert B., Hunter C. N. Blue shifts in bacteriochlorophyll absorbance correlate with changed hydrogen bonding patterns in light-harvesting 2 mutants of Rhodobacter sphaeroides with alterations at alpha-Tyr-44 and alpha-Tyr-45. Biochem J. 1994 May 1;299(Pt 3):695–700. doi: 10.1042/bj2990695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Frank H. A., Cogdell R. J. Carotenoids in photosynthesis. Photochem Photobiol. 1996 Mar;63(3):257–264. doi: 10.1111/j.1751-1097.1996.tb03022.x. [DOI] [PubMed] [Google Scholar]
  6. Ivancich A., Artz K., Williams J. C., Allen J. P., Mattioli T. A. Effects of hydrogen bonds on the redox potential and electronic structure of the bacterial primary electron donor. Biochemistry. 1998 Aug 25;37(34):11812–11820. doi: 10.1021/bi9806908. [DOI] [PubMed] [Google Scholar]
  7. Ivancich A., Lutz M., Mattioli T. A. Temperature-dependent behavior of bacteriochlorophyll and bacteriopheophytin in the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry. 1997 Mar 18;36(11):3242–3253. doi: 10.1021/bi962483i. [DOI] [PubMed] [Google Scholar]
  8. Lapouge K., Näveke A., Gall A., Ivancich A., Seguin J., Scheer H., Sturgis J. N., Mattioli T. A., Robert B. Conformation of bacteriochlorophyll molecules in photosynthetic proteins from purple bacteria. Biochemistry. 1999 Aug 24;38(34):11115–11121. doi: 10.1021/bi990723z. [DOI] [PubMed] [Google Scholar]
  9. Mattioli T. A., Hoffmann A., Robert B., Schrader B., Lutz M. Primary donor structure and interactions in bacterial reaction centers from near-infrared Fourier transform resonance Raman spectroscopy. Biochemistry. 1991 May 14;30(19):4648–4654. doi: 10.1021/bi00233a002. [DOI] [PubMed] [Google Scholar]
  10. Mattioli T. A., Williams J. C., Allen J. P., Robert B. Changes in primary donor hydrogen-bonding interactions in mutant reaction centers from Rhodobacter sphaeroides: identification of the vibrational frequencies of all the conjugated carbonyl groups. Biochemistry. 1994 Feb 22;33(7):1636–1643. doi: 10.1021/bi00173a004. [DOI] [PubMed] [Google Scholar]
  11. McAuley-Hecht K. E., Fyfe P. K., Ridge J. P., Prince S. M., Hunter C. N., Isaacs N. W., Cogdell R. J., Jones M. R. Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry. 1998 Apr 7;37(14):4740–4750. doi: 10.1021/bi971717a. [DOI] [PubMed] [Google Scholar]
  12. Mozhaev V. V., Heremans K., Frank J., Masson P., Balny C. High pressure effects on protein structure and function. Proteins. 1996 Jan;24(1):81–91. doi: 10.1002/(SICI)1097-0134(199601)24:1<81::AID-PROT6>3.0.CO;2-R. [DOI] [PubMed] [Google Scholar]
  13. Olsen J. D., Sockalingum G. D., Robert B., Hunter C. N. Modification of a hydrogen bond to a bacteriochlorophyll a molecule in the light-harvesting 1 antenna of Rhodobacter sphaeroides. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7124–7128. doi: 10.1073/pnas.91.15.7124. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Olsen J. D., Sturgis J. N., Westerhuis W. H., Fowler G. J., Hunter C. N., Robert B. Site-directed modification of the ligands to the bacteriochlorophylls of the light-harvesting LH1 and LH2 complexes of Rhodobacter sphaeroides. Biochemistry. 1997 Oct 14;36(41):12625–12632. doi: 10.1021/bi9710481. [DOI] [PubMed] [Google Scholar]
  15. Parson W. W., Chu Z. T., Warshel A. Electrostatic control of charge separation in bacterial photosynthesis. Biochim Biophys Acta. 1990 Jun 26;1017(3):251–272. doi: 10.1016/0005-2728(90)90192-7. [DOI] [PubMed] [Google Scholar]
  16. Parson W. W., Cogdell R. J. The primary photochemical reaction to bacterial photosynthesis. Biochim Biophys Acta. 1975 Mar 31;416(1):105–149. doi: 10.1016/0304-4173(75)90014-2. [DOI] [PubMed] [Google Scholar]
  17. Pieper J., Irrgang K. D., Rätsep M., Voigt J., Renger G., Small G. J. Assignment of the lowest Qy-state and spectral dynamics of the CP29 chlorophyll a/b antenna complex of green plants: a hole-burning study. Photochem Photobiol. 2000 May;71(5):574–581. doi: 10.1562/0031-8655(2000)071<0574:aotlqy>2.0.co;2. [DOI] [PubMed] [Google Scholar]
  18. Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 1987 Nov 1;166(2):368–379. doi: 10.1016/0003-2697(87)90587-2. [DOI] [PubMed] [Google Scholar]
  19. Sesselmann T, Richter W, Haarer D, Morawitz H. Spectroscopic studies of impurity-host interactions in dye-doped polymers: Hydrostatic-pressure effects versus temperature effects. Phys Rev B Condens Matter. 1987 Nov 15;36(14):7601–7611. doi: 10.1103/physrevb.36.7601. [DOI] [PubMed] [Google Scholar]
  20. Stowell M. H., McPhillips T. M., Rees D. C., Soltis S. M., Abresch E., Feher G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science. 1997 May 2;276(5313):812–816. doi: 10.1126/science.276.5313.812. [DOI] [PubMed] [Google Scholar]
  21. Sturgis J. N., Gall A., Ellervee A., Freiberg A., Robert B. The effect of pressure on the bacteriochlorophyll a binding sites of the core antenna complex from Rhodospirillum rubrum. Biochemistry. 1998 Oct 20;37(42):14875–14880. doi: 10.1021/bi9810003. [DOI] [PubMed] [Google Scholar]
  22. Sturgis J. N., Hagemann G., Tadros M. H., Robert B. Biochemical and spectroscopic characterization of the B800-850 light-harvesting complex from Rhodobacter sulphidophilus and its B800-830 spectral form. Biochemistry. 1995 Aug 22;34(33):10519–10524. doi: 10.1021/bi00033a025. [DOI] [PubMed] [Google Scholar]
  23. Sturgis J. N., Jirsakova V., Reiss-Husson F., Cogdell R. J., Robert B. Structure and properties of the bacteriochlorophyll binding site in peripheral light-harvesting complexes of purple bacteria. Biochemistry. 1995 Jan 17;34(2):517–523. doi: 10.1021/bi00002a016. [DOI] [PubMed] [Google Scholar]
  24. Sturgis J. N., Olsen J. D., Robert B., Hunter C. N. Functions of conserved tryptophan residues of the core light-harvesting complex of Rhodobacter sphaeroides. Biochemistry. 1997 Mar 11;36(10):2772–2778. doi: 10.1021/bi962524a. [DOI] [PubMed] [Google Scholar]
  25. Wachtveitl J., Farchaus J. W., Das R., Lutz M., Robert B., Mattioli T. A. Structure, spectroscopic, and redox properties of Rhodobacter sphaeroides reaction centers bearing point mutations near the primary electron donor. Biochemistry. 1993 Nov 30;32(47):12875–12886. doi: 10.1021/bi00210a041. [DOI] [PubMed] [Google Scholar]
  26. Wu H. M., Rätsep M., Young C. S., Jankowiak R., Blankenship R. E., Small G. J. High-pressure and stark hole-burning studies of chlorosome antennas from Chlorobium tepidum. Biophys J. 2000 Sep;79(3):1561–1572. doi: 10.1016/S0006-3495(00)76407-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Yeates T. O., Komiya H., Chirino A., Rees D. C., Allen J. P., Feher G. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions. Proc Natl Acad Sci U S A. 1988 Nov;85(21):7993–7997. doi: 10.1073/pnas.85.21.7993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Zou Wen, Hu Chun-hong, Zhou Jian-ping. [Relationship between the expression of E-cadherin-catenins and alpha-, beta-, gamma-catenin and the metastasis and prognosis of breast cancer]. Hunan Yi Ke Da Xue Xue Bao. 2002 Dec 28;27(6):499–502. [PubMed] [Google Scholar]

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