Role of the hydrogen bond from Leu722 to the A1A phylloquinone in photosystem I

Biochemistry

Volumn 48, Issue 15, 2009, Pages 3315-3324

  Srinivasan, Nithya ^a   Karyagina, Irina ^b   Bittl, Robert ^b   Van Der Est, Art ^c   Golbeck, John H ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

^c BROCK UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CARBONYL GROUPS; COFACTORS; ELECTRON TRANSFERS; EPR SIGNALS; EPR STUDIES; H BONDINGS; HYPERFINE COUPLINGS; LIGHT INTENSITIES; LOW TEMPERATURES; MIDPOINT POTENTIALS; NUMERICAL SIMULATIONS; PHOTOSYSTEM I; PHYLLOQUINONE; POLARIZATION PATTERNS; RADICAL PAIRS; REDUCTION BEHAVIORS; REVERSIBLE ELECTRON TRANSFERS; SODIUM DITHIONITE; WILD TYPES;

COUPLINGS; ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSITIONS; FREE RADICAL REACTIONS; HYDROGEN; HYDROGEN BONDS; ISOMERS; PARAMAGNETIC RESONANCE; POLARIZATION; QUANTUM THEORY; SODIUM; SPIN DYNAMICS;

KETONES;

CARBONYL DERIVATIVE; LEUCINE; PHYTOMENADIONE; QUINONE DERIVATIVE; SODIUM DITHIONITE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; AMPLITUDE MODULATION; ARTICLE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; HYDROGEN BOND; LIGHT INTENSITY; PHOTOSYSTEM I; POLARIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTON TRANSPORT; REDUCTION; SIGNAL TRANSDUCTION; TEMPERATURE; WILD TYPE;

AMINO ACID SUBSTITUTION; CRYSTALLOGRAPHY, X-RAY; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICALS; HYDROGEN BONDING; LEUCINE; OXIDATION-REDUCTION; PHOTOSYSTEM I PROTEIN COMPLEX; POINT MUTATION; SYNECHOCYSTIS; TEMPERATURE; TRYPTOPHAN; VITAMIN K 1;

EID: 65249176799     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802340s     Document Type: Article

References (47)

1. Schubert, W. D., Klukas, O., Saenger, W., Witt, H. T., Fromme, P., and Krauss, N. (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.
2. Chitnis, P. R., Xu, Q., Chitnis, V. P., and Nechushtai, R. (1995) Function and organization of Photosystem I polypeptides. Photosynth. Res. 44, 23-40.
3. Jordan, P., Fromme, P., Witt, H. T., Klukas, O., Saenger, W., and Krauβ, N. (2001) Three dimensional structure of Photosystem I at 2.5 Å resolution. Nature 411, 909-917.
4. Guergova-Kuras, M., Boudreaux, B., Joliot, A., Joliot, P., and Redding, K. (2001) Evidence for two active branches for electron transfer in Photosystem I. Proc. Natl. Acad. Sci. U.S.A. 98, 4437-4442.
5. Joliot, P., and Joliot, A. (1999) In vivo analysis of the electron transfer within Photosystem I: are the two phylloquinones involved? Biochemistry 38, 11130-11136.
6. Bautista, J. A., Rappaport, F., Guergova-Kuras, M., Cohen, R. O., Golbeck, J. H., Wang, J. Y., Beal, D., and Diner, B. A. (2005) Biochemical and biophysical characterization of Photosystem I from phytoene desaturase and zeta-carotene desaturase deletion mutants of Synechocystis sp. PCC 6803: Evidence for PsaA- and PsaB-side electron transport in cyanobacteria. J. Biol. Chem. 280, 20030-20041.
7. .- radical pair for photosynthetic electron transfer on both the PsaA and PsaB branches of the Photosystem I reaction centre. FEBS Lett. 503, 56-60.
8. - in spin-correlated radical pairs. Biochemistry 44, 2119-2128.
9. - radical pair of Photosystem I indicates that both reaction center subunits are competent in electron transfer in cyanobacteria, green algae, and higher plants. Biochemistry 45, 7389-7403.
10. -, the reduced secondary electron acceptor in Photosystem I. Biochemistry 37, 9466-9476.
11. 1 in Photosystem I: only the slower phase is activated. Biochim. Biophys. Acta 1604, 7-12.
12. X. Biochim. Biophys. Acta 1708, 283-310.
13. Ishikita, H., and Knapp, E. W. (2003) Redox potential of quinones in both electron transfer branches of Photosystem I. J. Biol. Chem. 278, 52002-52011.
14. Boudreaux, B., MacMillan, F., Teutloff, C., Agalarov, R., Gu, F., Grimaldi, S., Bittl, R., Brettel, K., and Redding, K (2001) Mutations in both sides of the Photosystem I reaction center identify the phylloquinone observed by electron paramagnetic resonance spectroscopy. J. Biol. Chem. 276, 37299-37306.
15. X. J. Biol. Chem. 278, 27864-27875.
16. X. J. Biol. Chem. 278, 27876-27887.
17. Purton, S., Stevens, D. R., Muhiuddin, I. P., Evans, M. C., Carter, S., Rigby, S. E., and Heathcote, P. (2001) Site-directed mutagenesis of PsaA residue W693 affects phylloquinone binding and function in the Photosystem I reaction center of Chlamydomonas reinhardtii. Biochemistry 40, 2167-2175.
18. 1 in Photosystem I after treatment in darkness at low redox potential. Biochim. Biophys. Acta 1057, 331-336.
19. 2 symmetry in the Photosystem I reaction center. Biochim. Biophys. Acta 1144, 54-61.
20. Poluektov, O. G., Paschenko, S. V., Utschig, L. M., Lakshmi, K. V., and Thurnauer, M. C. (2005) Bidirectional electron transfer in Photosystem I: direct evidence from high-frequency time-resolved EPR spectroscopy. J. Am. Chem. Soc. 127, 11910-11911.
21. Stehlik, D. (2006) Transient EPR spectroscopy as applied to lightinduced functional intermediates along the electron transfer pathway in Photosystem I, in Photosystem I: The Light-DriVen Plastocyanin: Ferredoxin Oxidoreductase (Golbeck, J., Ed.) pp 361-386, Springer, Dordrecht.
22. Rigby, S. E., Evans, M. C., and Heathcote, P. (2001) Electron nuclear double resonance (ENDOR) spectroscopy of radicals in Photosystem I and related Type 1 photosynthetic reaction centres. Biochim. Biophys. Acta 1507, 247-259.
23. 13C labelled naphthoquinones and transient EPR. Appl. Magn. Reson. 30, 287-310.
24. 13C labeled naphthoquinones. J. Phys. Chem. B 108, 9439-9448.
25. Feldman, K. S., Hester, D. K., 2nd, and Golbeck, J. H. (2007) A relationship between amide hydrogen bond strength and quinone reduction potential: Implications for Photosystem I and bacterial reaction center quinone function. Bioorg. Med. Chem. Lett. 17, 4891-4894.
26. - in Photosystem I from the orientation of the magnetic interaction tensors. J. Phys. Chem. B 104, 9728-9739.
27. Kandrashkin, Y. E., Vollmann, W., Stehlik, D., Salikhov, K., and van der Est, A. (2002) The magnetic field dependence of the electron spin polarization in consecutive spin correlated radical pairs in type I photosynthetic reaction centres. Mol. Phys. 100, 1431-1443.
28. 1 site in Photosystem I in spinach and cyanobacteria. Biochim. Biophys. Acta 1320, 195-207.
29. 1 site of Phototsystem I. An electron spin polarization electron paramagnetic resonance study. Biochim. Biophys. Acta 1011, 311-320.
30. + in Photosystem I: A single crystals EPR and ENDOR study. J. Phys. Chem. B 105, 1225-1239.
31. Webber, A. N., and Lubitz, W. (2001) P700: the primary electron donor of Photosystem I. Biochim. Biophys. Acta 1507, 61-79.
32. -in bacterial reaction centers. J. Phys. Chem. B 101, 1437-1443.
33. 1) acceptor in cyanobacterial Photosystem I, in Photosynthesis. Energy from the sun: 14th International Congress on Photosynthesis (Allen, J. F., Gantt, E., Golbeck, J. H., and Osmond, B., Eds.) pp 207-210, Springer, Dordrecht.
34. Polm, M., and Brettel, K. (1998) Secondary pair charge recombination in Photosystem I under strongly reducing conditions: Temperature dependence and suggested mechanism. Biophys. J. 74, 3173-3181.
35. x in Photosystem I. Biochemistry 41, 394-405.
36. 1B phylloquinones in Photosystem I. Biochim. Biophys. Acta, submitted.
37. Pushkar, Y. N., Zech, S. G., Stehlik, D., Brown, S., van der Est, A., and Zimmermann, H. (2002) Orientation and protein-cofactor interactions of monosubstituted n-alkyl naphthoquinones in the A1 binding site of Photosystem I. J. Phys. Chem. B 106, 12052-12058.
38. 1 site of Photosystem I. Altered kinetics of electron transfer in phylloquinone biosynthetic pathway mutants studied by timeresolved optical, EPR, and electrometric techniques. J. Biol. Chem. 275, 23429-23438.
39. B and containing plastoquinone or exchanged 9,10-anthraquinone. J. Biol. Chem. 280, 12371-12381.
40. 1 site of Photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275, 8523-8530.
41. 1 site of Photosystem I. II. Structural and functional characterization of phylloquinone biosynthetic pathway mutants by electron paramagnetic resonance and electron-nuclear double resonance spectroscopy. J. Biol. Chem. 275, 8531-8539.
42. 1 site of Photosystem I. In vivo replacement of plastoquinone-9 by media-supplemented naphthoquinones in phylloquinone biosynthetic pathway mutants of Synechocystis sp. PCC 6803. J. Biol. Chem. 276, 31512-31521.
43. 1 in Photosystem I of the cyanobacterium Synechocystis 6803. Biochemistry 27, 1494-1500.
44. 1 as studied by time resolved EPR. FEBS Lett. 284, 98-102.
45. van der Est, A., Sieckmann, I., Lubitz, W., and Stehlik, D. (1995) Differences in the binding of the quinone acceptor in Photosystem I and reaction centers of Rhodobacter Sphaeroides-R26 studied with transient EPR spectroscopy. Chem. Phys. 194, 349-360.
46. 1 site as studied by transient EPR. J. Biol. Chem. 280, 12382-12390.
47. 1 in intact spinach chloroplasts and cyanobacteria in ViVo. Biochim. Biophys. Acta 1318, 133-144.