Photosynthetica 2006, 44(3):433-438 | DOI: 10.1007/s11099-006-0047-0

Temperature dependent UV-Vis spectral changes in hydrogen-and deuterium-bonded photosynthetic reaction centers of Rhodobacter sphaeroides

A. E. Ostafin1,3, J. A. Popova1, C. K. Payne1, H. Mizukami2, J. R. Norris Jr.1
1 Department of Chemistry, University of Chicago, Chicago, USA
2 Department of Biological Sciences, Wayne State University, Detroit, USA
3 Chemical & Biomolecular Engineering, University of Notre Dame, Notre Dame, USA

The UV-Vis absorption spectra of detergent-isolated hydrogen-and deuterium-bonded reaction centers (RCs) from Rhodobacter sphaeroides PUC 705Ba were examined as a function of temperature between 20 and 55 °C. The enthalpy and entropy of denaturation for the specimens was determined, revealing that their process of thermal denaturation is significantly different. Deuterium-bonded RCs are most stable at 37 °C, rather than at room temperature, and undergo a "cold denaturation" as the temperature is lowered to room temperature. At room temperature the addition of 1,3,5-heptanetriol brought the deuterium-bonded RC back to its more stable configuration. Hence the hydrogen bonding interactions in the RC do influence its conformation and this is reflected in the microenvironment of its associated pigments.

Additional key words: enthalpy; entropy; ferricyanide; 1,3,5-hexanetriol; photosynthetic bacteria

Received: August 10, 2005; Accepted: March 2, 2006; Published: September 1, 2006  Show citation

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Ostafin, A.E., Popova, J.A., Payne, C.K., Mizukami, H., & Norris, J.R. (2006). Temperature dependent UV-Vis spectral changes in hydrogen-and deuterium-bonded photosynthetic reaction centers of Rhodobacter sphaeroides. Photosynthetica, 44(3), 433-438. doi: 10.1007/s11099-006-0047-0
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    References

    1. Angerhofer, A.: Chlorophyll triplets and radical pairs.-In: Scheer, H. (ed.): Chlorophylls. Pp. 945-991. CRC Press, Boca Raton-Boston-London 1991.
    2. Babu, C.R., Hilser, V.J., Wand, A.J.: Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation.-Nature struct. mol. Biol. 11: 352-357, 2004. Go to original source...
    3. Bohr, J.: Phonon forces and cold denaturation.-Int. J. Quant. Chem. 92: 118-122, 2003. Go to original source...
    4. Brandts, J.F.: Structure and Stability of Biological Macromolecules.-Marcel Dekker, New York 1969.
    5. Chang, C.-H., El-Kabbani, O., Tiede, D., Norris, J., Schiffer, M.: Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.-Biochemistry 30: 5352-5360, 1991. Go to original source...
    6. Crespi, H.L., Norris, J.R., Katz, J.J.: Effect of isotopic substitution on the electron spin resonance spectra of flavin and flavoprotein free radicals.-Biochim. biophys. Acta 253: 509-513, 1971. Go to original source...
    7. Deisenhofer, J., Epp, O., Sinning, I., Michel, H.: Crystallographic refinement at 2.4 Å resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis.-J. mol. Biol. 246: 429-457, 1995. Go to original source...
    8. Hayashi, H., Miyao, M., Morita, S.: Absorption and fluorescence spectra of light-harvesting bacteriochlorophyll-protein complexes from Rhodopseudomonas palustris in the near-infrared region.-J. Biochem. (Tokyo) 91: 1017-1027, 1982. Go to original source...
    9. Klotz, I.M., Darnall, D.W., Langerman, N.L.: The Proteins.-Academic Press, New York 1974.
    10. Lancaster, C.R., Bibikova, M.V., Sabatino, P., Oesterhelt, D., Michel, H.: Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution.-J. biol. Chem. 275: 39364-39368, 2000. Go to original source...
    11. Norris, J.R., Crespi, H.L., Katz, J.J.: Characterization of a new photo-ESR signal associated with photosynthesis.-Biochem. biophys. Res. Commun. 49: 139-146, 1972. Go to original source...
    12. Norris, J.R., Uphaus, R.A., Crespi, H.L., Katz, J.J.: Electron spin resonance of chlorophyll and the origin of signal I in photosynthesis.-Proc. nat. Acad. Sci. USA 68: 625-628, 1971. Go to original source...
    13. Norris, J.R., Uphaus, R.A., Katz, J.J.: Electron spin resonance in 13C-labeled chlorophyll and 13C-labeled algae.-Biochim. biophys. Acta 275: 161-168, 1972. Go to original source...
    14. Ostafin, A.E., Weber, S.: Quinone exchange in photosystem I of spinach and cyanobacteria.-Biochim. biophys. Acta 1320: 195-208, 1997. Go to original source...
    15. Pashchenko, V.Z.: [Relation between structural and dynamic organization and picosecond steps of photosynthesis in Rhodobacter sphaeroides reaction centers.]-Biofizika 45: 461-468, 2000. [In Russ.]
    16. Scheiner, S., Cuma, M.: Relative stability of hydrogen and deuterium bonds.-J. amer. chem. Soc. 118: 1511-1521, 1996. Go to original source...
    17. Schenck, C.C., Parson, W.W., Holten, D., Windsor, M.W., Sarai, A.: Temperature dependence of electron transfer between bacteriopheophytin and ubiquinone in protonated and deuterated reaction centers of Rhodopseudomonas sphaeroides.-Biophys. J. 36: 479-89, 1981. Go to original source...
    18. Schulz, G.E., Schirmer, R.H.: Principles of Protein Structure.-Springer-Verlag, New York 1979. Go to original source...
    19. Thompson, L.K., Blaylock, R., Sturtevant, J.M., Brudvig, G.W.: Molecular basis for the heat denaturation of photosystem II.-Biochemistry 28: 6686-6695, 1989. Go to original source...
    20. Yakovlev, A.G., Shuvalov, V.A.: Electron transfer in deuterated reaction centers of Rhodobacter sphaeroides at 90 K according to femtosecond spectroscopy data.-Biochemistry 68: 603-610, 2003.
    21. Yokogaki, S., Unno, K., Oku, N., Okada, S.: Chaperonin-repairable subtle incompleteness of protein assembly induced by a substitution of hydrogen with deuterium: effect of GroE on deuterated ribulose 1,5-bisphosphate.-Plant Cell Physiol. 36: 419-423, 1995. Go to original source...

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