Coupling of light-induced electron transfer to proton uptake in photosynthesis

Nature Structural Biology

Volumn 10, Issue 8, 2003, Pages 637-644

  Remy, André ^a   Gerwert, Klaus ^a  

^a RUHR UNIVERSITY BOCHUM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLUTAMINE; HISTIDINE;

ARTICLE; BIOTRANSFORMATION; ELECTRON; ELECTRON TRANSPORT; ENERGY; INFRARED SPECTROSCOPY; PHASE TRANSITION; PHOTOSYNTHESIS; PRIORITY JOURNAL; PROTEIN SYNTHESIS; PROTON TRANSPORT; REDUCTION;

ELECTRON TRANSPORT; KINETICS; LIGHT; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PHOTOSYNTHESIS; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; PROTON-MOTIVE FORCE; QUINONES; RHODOBACTER SPHAEROIDES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

MUS;

EID: 0041622652     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb954     Document Type: Article

References (53)

1. Okamura, M.Y., Paddock, M.L., Graige, M.S. & Feher, G. Proton and electron transfer in bacterial reaction centers. Biochim. Biophys. Acta 1458, 148-163 (2000).
2. Gerwert, K. Molecular reaction mechanisms of proteins as monitored by time-resolved FTIR spectroscopy. Curr. Opin. Struct. Biol. 3, 769-773 (1993).
3. Mäntele, W. Infrared and Fourier-transform infrared spectroscopy. In Biophysical Techniques in Photosynthesis (eds. Amesz, J. & Hoff, A.J.) 137-160 (Kluwer, Dordrecht, Netherlands, 1996).
4. Vogel, R. & Siebert, F. Vibrational spectroscopy as a tool for probing protein function. Curr. Opin. Chem. Biol. 4, 518-523 (2000).
5. Barth, A. & Zscherp, C. What vibrations tell us about proteins. Quart. Rev. Biophysics 35, 369-430 (2002).
6. Stowell, M.H.B. et al. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science 276, 812-816 (1997).
7. Zouni, A. et al. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409, 739-743 (1997).
8. Feher, G., Allen, J.P., Okamura, M.Y. & Rees, D.C. Structure and function of bacterial photosynthetic reaction centres. Nature 339, 111-116 (1989).
9. Ermler, U., Fritzsch, G., Buchanan, S. & Michel, H. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure 2, 925-936 (1994).
10. Kuglstatter, A., Ermler, U., Michel, H., Baciou, L. & Fritzsch, G. X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: structural changes induced by point mutations at position L209 modulate electron and proton transfer. Biochemistry 40, 4253-4260 (2001).
11. A in Rhodobacter sphaeroides R26 reaction centres monitored by Fourier transform infrared spectroscopy using site-specific isotopically labelled ubiquinone-10. EMBO J. 13, 5523-5530 (1994).
12. 13C-labeled ubiquinone. Biochemistry 33, 14378-14386 (1994).
13. B carbonyl groups in Rhodobacter sphaeroides R26 reaction centres. FEBS Lett. 370, 88-92 (1995).
14. B vibrations in Rhodobacter sphaeroides and Rhodopseudomonas viridis probed by isotope labeling. Biochemistry 34, 11606-11616 (1995).
15. Holzapfel, W. et al. Initial electron-transfer in the reaction center from Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA 87, 5168-5172 (1990)
16. Gray, H.B. & Winkler, J.R. Electron transfer in proteins. Ann. Rev. Biochem. 65, 537-561 (1995).
17. Moser, C.C., Page, C.C., Farid, R. & Dutton, P.L. Biological electron transfer. J. Bioenerg. Biomembr. 27, 263-274 (1995).
18. 2+. Biochemistry 25, 2276-2287 (1986).
19. Tiede, D. Vázquez, J., Córdova, J. & Marone, P.A. Time-resolved electrochromism associated with the formation of quinone anions in Rhodobacter sphaeroides R-26 reaction center. Biochemistry 35, 10763-10775 (1996).
20. - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay. Proc. Natl. Acad. Sci. USA 95, 11679-11684 (1998).
21. - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers. Biochemistry 37, 2818-2829 (1998).
22. - in Rhodobacter sphaeroides reaction centers. Biochemistry 39, 7445-7454 (2000).
23. Gerwert, K. Molecular reaction mechanisms of proteins monitored by time-resolved FTIR difference spectroscopy. In Handbook of Vibrational Spectroscopy (eds. Chalmers, J.M. & Griffiths, P.R.) (Wiley, Chichester, UK, 2001).
24. B reduction, Biochemistry 31, 5799-5808 (1992).
25. - formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy. Biochemistry 34, 2832-2843 (1995).
26. Uhmann, W., Becker, A., Taran, C. & Siebert, F. Time-resolved FT-IR absorption spectroscopy using a step-scan interferometer. Appl. Spectrosc. 45, 390-397 (1991).
27. Burie, J.-R., Leibl, W., Nabedryk, E. & Breton, J. Step-scan FT-IR spectroscopy of electron transfer in the photosynthetic bacterial reaction center. Appl. Spectrosc. 47, 1401-1404 (1993).
28. Rammelsberg, R., Hessling, B., Chorongiewski, H. & Gerwert, K. Molecular reaction mechanisms of proteins monitored by nanosecond step-scan FT-IR difference spectroscopy. Appl. Spectrosc. 51, 558-562 (1997).
29. B-transition in Rb. sphaeroides R26 reaction centres. Photosynth. Res. 55, 261-266 (1998).
30. Hessling, B., Souvignier, G. & Gerwert, K. A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates. Biophysical J. 65, 1929-1941 (1993).
31. Gerwert, K., Souvignier, G. & Hess, B. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy. Proc. Natl. Acad. Sci. USA 87, 9774-9778 (1990).
32. 1 early intermediate of photoactive yellow protein by FTIR spectroscopy. Nat. Struct. Biol. 8, 265-270 (2001).
33. Nabedryk, E. et al. A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center. FEBS Lett. 266, 59-62 (1990).
34. Kleinfeld, D., Okamura, M.Y. & Feher, G. Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes. Biochemistry 23, 5780-5786 (1984).
35. 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 30, 1243-1257 (1990).
36. Nabedryk, E. et al. Fourier transform infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides. Biochemistry 34, 14722-14732 (1995).
37. A demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides. Biochemistry 36, 4515-4525 (1997).
38. Rammelsberg, R., Huhn, G., Lübben, M. & Gerwert, K. Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network. Biochemistry 37, 5001-5009 (1998).
39. B. Structure 5, 1339-1359 (1997).
40. Noguchi, T., Inoue, Y. & Tang, X.-S. Structure of a histidine ligand in the photosynthetic oxygen-evolving complex as studied by light-induced Fourier transform infrared difference spectroscopy. Biochemistry 38, 10187-10195 (1999).
41. Hasegawa, K., Ono, T. & Noguchi, T. Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: infrared and raman markers of the protonation state of a histidine side chain. J. Phys. Chem. B. 104, 4253-4265 (2000).
42. 2+ in bacterial reaction centers. Proc. Natl. Acad. Sci. USA 97, 1542-1547 (2000).
43. Ädelroth, P. et al. Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors. Biochemistry 40, 14538-14546 (2001).
44. B). Biochemistry 40, 6893-6902 (2001).
45. B in Rhodobacter sphaeroides reaction centers. Biochim. Biophys. Acta 1553, 320-330 (2002).
46. B in reaction centers from Rhodobacter sphaeroides. Biochemistry 40, 13826-13832 (2001).
47. + binding by bacterial photosynthetic reaction centers: comparison of spectrophotometric and conductimetric methods. Biochim. Biophys, Acta 934, 314-328 (1988).
48. B binding site at the proximal position in wild-type reaction centers and in the Pro-L209 → Tyr mutant from Rhodobacter sphaeroides. Biochemistry 41, 12921-12927 (2002).
49. Spassov, V.Z., Luecke, H., Bashford, D. & Gerwert, K. pKa calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin. J. Mol. Biol. 312, 203-219 (2001).
50. Nugent, J.H.A. Oxygenic photosynthesis - electron transfer in photosystem I and photosystem II. Eur. J. Biochem. 237, 519-531 (1996).
51. Farchaus, J.W. & Oesterhelt, D. A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3 kb puf operon shuttle fragment. EMBO J. 8, 47-54 (1989).
52. --Übergang im bakteriellen photosynthetischen Reaktionszentrum von Rhodobacter sphaeroides. Thesis, Ruhr-University Bochum, Bochum, Germany (2002).
53. Okamura, M.Y., Isaacson, R.A. & Feher, G. Primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides. Proc. Nat. Acad. Sci. USA 72, 3491-3495 (1975).