Light- and redox-dependent thermal stability of the reaction center of the photosynthetic bacterium Rhodobacter sphaeroides

Photochemistry and Photobiology

Volumn 75, Issue 6, 2002, Pages 605-612

  Tokaji, Zsolt ^a   Tandori, Júlia ^c   Maróti, Péter ^b  

^a INSTITUTE OF BIOCHEMISTRY   (Hungary)

^b UNIVERSITY OF SZEGED   (Hungary)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIOCHLOROPHYLL; BACTERIOPHEOPHYTIN; UBIDECARENONE; BACTERIOCHLOROPHYLL B;

ARTICLE; LIGHT; NONHUMAN; OXIDATION REDUCTION REACTION; PHOTOSYNTHESIS; PHOTOTROPHIC BACTERIUM; RHODOPSEUDOMONAS SPHAEROIDES; TEMPERATURE; THERMODYNAMICS; THERMOSTABILITY; CHEMISTRY; HEAT; KINETICS; LIGHT HARVESTING SYSTEM; METABOLISM; RADIATION EXPOSURE; RHODOBACTER SPHAEROIDES;

BACTERIA (MICROORGANISMS); PHOTOBACTERIA; RHODOBACTER; RHODOBACTER SPHAEROIDES; RHODOPSEUDOMONAS;

BACTERIOCHLOROPHYLLS; HEAT; KINETICS; LIGHT; LIGHT-HARVESTING PROTEIN COMPLEXES; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; RHODOBACTER SPHAEROIDES; THERMODYNAMICS;

EID: 0036594522     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2002)075<0605:LARDTS>2.0.CO;2     Document Type: Article

References (43)

1. Yamashita, T. and W. L. Butler (1968) Inhibition of chloroplasts by UV-irradiation and heat-treatment. Plant Physiol. 43, 2037-2040.
2. Barber, J. and B. Andersson (1992) Too much of a good thing: light can be bad for photosynthesis. Trends Biochem. Sci. 17, 61-66.
3. Yamane, Y., Y. Kashino, H. Koike and K. Satoh (1998) Effects of high temperatures on the photosynthetic systems in spinach: oxygen-evolving activities, fluorescence characteristics and the denaturation process. Photosynth. Res. 57, 51-59.
4. Cogdell, R. J. and H. A. Frank (1987) How carotenoids function in photosynthetic bacteria. Biochim. Biophys. Acta 895, 63-79.
5. Demmig-Adams, B. (1990) Carotenoids and photoprotection in plants: a role for the xanthophyll zeaxanthin. Biochim. Biophys. Acta 1020, 1-24.
6. Griffiths, M., W. R. Sistrom, G. Cohen-Bazire and R. Y. Stanier (1995) Function of carotenoids in photosynthesis. Nature 176, 1211-1214.
7. Frank, H. A. and R. J. Cogdell (1996) Carotenoids in photosynthesis. Photochem. Photobiol. 63, 257-264.
8. Castenholz, R. W. and B. K. Pierson (1995) Ecology of thermophilic anoxygenic phototrophs. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan and C. E. Bauer), pp. 87-103. Kluwer Academic Publishers, Dordrecht.
9. Tandori, J., E. Hideg, L. Nagy, P. Maróti and I. Vass (2001) Photoinhibition of carotenoidless reaction centers from Rhodobacter sphaeroides by visible light. Effect on protein structure and electron transport. Photosynth. Res. 70, 175-184.
10. Aro, M. E., I. Virgin and B. Andersson (1993) Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta 1143, 113-134.
11. Durrant, J. R., L. B. Giorgi, J. Barber, D. R. Klug and G. Porter (1990) Characterization of triplet states in isolated photosystem II reaction centres: oxygen quenching as a mechanism for photodamage. Biochim. Biophys. Acta 1017, 167-175.
12. Hideg, E., C. Spetea and I. Vass (1994) Singlet oxygen and free radical production during acceptor and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy. Biochim. Biophys. Acta 1186, 143-152.
13. Shinkarev, V. P. and C. A. Wraight (1993) Electron and proton transfer in the acceptor quinone complex of reaction centers of phototropic bacteria. In The Photosynthetic Reaction Center, Vol. I (Edited by J. Deisenhofer and J. R. Norris), pp. 23-42. Academic Press Inc., San Diego.
14. Okamura, M. Y., R. A. Isaacson and G. Feher (1979) Spectroscopic and kinetic properties of the transient intermediate acceptor in reaction centers of Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 546, 394-417.
15. Dancsházy, Zs., Zs. Tokaji and A. Dér (1999) Bleaching of bacteriorhodopsin by continuous light. FEBS Lett. 450, 154-157.
16. Simidjiev, I., V. Barzda, L. Mustardy and G. Garab (1998) Role of thylakoid lipids in the structural flexibility of lamellar aggregates of the isolated light-harvesting chlorophyll a/b complex of photosystem II. Biochemistry 37, 4169-4173.
17. - from excited reaction centers of Rhodobacter sphaeroides. J. Am. Chem. Soc. 122, 1479-1485.
18. Nagy, L., V. Kiss, V. Brumfeld and S. Malkin (2001) Thermal and structural changes of photosynthetic reaction centers characterized by photoacoustic detection with a broad frequency band hydrophone. Photochem. Photobiol. 74, 81-87.
19. Brzezinski, P. and L. E. Andreasson (1995) Trypsin treatment of reaction centers from Rhodobacter sphaeroides in the dark and under illumination: protein structural changes follow charge separation. Biochemistry 34, 7498-7506.
20. Stowell, M. H. B., T. M. McPhillips, D. C. Rees, S. M. Soltis, E. Abresch and G. Feher (1997) Light induced structural changes and mechanism of electron/proton transfer in the photosynthetic reaction center. Science 276, 812-816.
21. B. Structure 5, 1339-1359.
22. - in bacterial reaction centers: measurement of light-induced electrogenic events in RCs incorporated in a phospholipid monolayer. In The Photosynthetic Bacterial Reaction Center II: Structure, Spectroscopy and Dynamics (Edited by J. Breton and A. Vermeglio), pp. 321-330. Plenum Press, New York.
23. Tiede, D. M. and D. K. Hanson (1992) Protein relaxation following quinon reduction in Rb. capsulatus: detection of likely protonation linked optical absorbance changes of the chromophores. In The Photosynthetic Bacterial Reaction Center II: Structure, Spectroscopy and Dynamics (Edited by J. Breton and A. Vermeglio), pp. 341-350. Plenum Press, New York.
24. Kálmán, L., K. Turzó and P. Maróti (1993) Probing reaction protonation by electrochromic absorption changes of cofactors in Rhodobacter sphaeroides. Photosynthetica 28, 185-194.
25. Kálmán, L. and P. Maróti (1997) Conformation-actived protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides. Biochemistry 36, 15269-15276.
26. 562 from Escherichia coli. Biochemistry 30, 10012-10018.
27. Andersson, B. and S. Styring (1991) Photosystem II: molecular organization, function and acclimation. Curr. Top. Bioenerg. 16, 1-81.
28. Barber, J. (1998) Photosystem two. Biochim. Biophys. Acta 1365, 269-277.
29. Schubert, W. D., O. Klukas, W. Saenger, H. T. Witt, P. Fromme and N. Krauss (1998) A common ancestor for oxygenic and anoxygenic photosynthetic systems: a comparison based on the structural model of photosystem I. J. Mol. Biol. 280, 297-314.
30. Blankenship, R. E. (2001) Molecular evidence for the evolution of photosynthesis. Trends Plant Sci. 6, 4-6.
31. + binding by bacterial photosynthetic reaction centers: comparison of spectrophotometric and conductometric methods. Biochim. Biophys. Acta 934, 314-328.
32. O'Reilly, J. E. (1973) Oxidation-reduction potential of the ferroferricyanide system in buffer solutions. Biochim. Biophys. Acta 292, 509-515.
33. Clayton, R. K. (1980) Photosynthesis: Physical Mechanisms and Chemical Patterns, Cambridge University Press, Cambridge.
34. B. Biochim. Biophys. Acta 766, 126-140.
35. Maróti, P. (1991) Electron transfer and proton uptake of photosynthetic bacterial reaction centres reconstituted in phospholipid vesicles. J. Photochem. Photobiol. B: Biol. 8, 263-277.
36. Senge, M. O. and K. M. Smith (1995) Biosynthesis and structures of the bacteriochlorophylls. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan and C. E. Bauer), pp. 137-151. Kluwer Academic Publishers, Dordrecht.
37. A species promote chlorophyll triplet formation. Proc. Natl. Acad. Sci. USA 89, 1408-1412.
38. Frauenfelder, H. (1995) The complexity of proteins. In Physics of Biological Systems (Edited by H. Flyvbjerg, J. Hertz, M. H. Jensen, O. G. Mouritsen and K. Sneppen), pp. 29-60. Springer, Berlin.
39. Freire, E. (1995) Thermal denaturation methods in the study of protein folding. In Methods in Enzymology, Energetics of Biological Macromolecules, Vol. 259 (Edited by M. L. Johnson and G. K. Ackers), pp. 144-168. Academic Press Inc., San Diego.
40. Baldwin, R. L. (1986) Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. USA 83, 8069-8072.
41. Hong, S. K., S. A. Pawlikowski, K. A. Vander Meulen and C. F. Yocum (2001) The oxidation state of the photosystem II manganese cluster influences the structure of the manganese stabilizing protein. Biochim. Biophys. Acta 1504, 262-274.
42. Lett, C. M., A. M. Berghuis, H. E. Frey, J. R. Lepock and J. G. Guillemette (1996) The role of a conserved water molecule in the redox-dependent thermal stability of iso-1-cytochrome c. J. Biol. Chem. 271, 29088-29093.
43. Lett, C. M., M. D. Rosu-Myles, H. E. Frey and J. G. Guillemette (1999) Rational design of a more stable yeast iso-1-cytochrome c. Biochim. Biophys. Acta - Protein Struct. Mol. Enzymol. 1432, 40-48.