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968 related items for PubMed ID: 19496556

  • 1. Proton-transfer reactions in reaction center of photosynthetic bacteria Rhodobacter sphaeroides.
    Kaneko Y, Hayashi S, Ohmine I.
    J Phys Chem B; 2009 Jul 02; 113(26):8993-9003. PubMed ID: 19496556
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  • 2. Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: dependence on protonation of Glu-L212 and Asp-L213.
    Ishikita H, Morra G, Knapp EW.
    Biochemistry; 2003 Apr 08; 42(13):3882-92. PubMed ID: 12667079
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  • 3. Simulating proton translocations in proteins: probing proton transfer pathways in the Rhodobacter sphaeroides reaction center.
    Sham YY, Muegge I, Warshel A.
    Proteins; 1999 Sep 01; 36(4):484-500. PubMed ID: 10450091
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  • 5. Proton and electron transfer to the secondary quinone (QB) in bacterial reaction centers: the effect of changing the electrostatics in the vicinity of QB by interchanging asp and glu at the L212 and L213 sites.
    Paddock ML, Feher G, Okamura MY.
    Biochemistry; 1997 Nov 18; 36(46):14238-49. PubMed ID: 9369497
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  • 9. Monitoring the pH dependence of IR carboxylic acid signals upon Q(B)- formation in the Glu-L212 --> Asp/Asp-L213 --> Glu swap mutant reaction center from Rhodobacter sphaeroides.
    Nabedryk E, Paddock ML, Okamura MY, Breton J.
    Biochemistry; 2007 Feb 06; 46(5):1176-82. PubMed ID: 17260947
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  • 10. The unusually strong hydrogen bond between the carbonyl of Q(A) and His M219 in the Rhodobacter sphaeroides reaction center is not essential for efficient electron transfer from Q(A)(-) to Q(B).
    Breton J, Lavergne J, Wakeham MC, Nabedryk E, Jones MR.
    Biochemistry; 2007 Jun 05; 46(22):6468-76. PubMed ID: 17497939
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  • 11. Identification of a novel protonation pattern for carboxylic acids upon Q(B) photoreduction in Rhodobacter sphaeroides reaction center mutants at Asp-L213 and Glu-L212 sites.
    Nabedryk E, Breton J, Okamura MY, Paddock ML.
    Biochemistry; 2004 Jun 15; 43(23):7236-43. PubMed ID: 15182169
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  • 12. Mechanism of proton transfer inhibition by Cd(2+) binding to bacterial reaction centers: determination of the pK(A) of functionally important histidine residues.
    Paddock ML, Sagle L, Tehrani A, Beatty JT, Feher G, Okamura MY.
    Biochemistry; 2003 Aug 19; 42(32):9626-32. PubMed ID: 12911304
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  • 13. Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers.
    Zhu Z, Gunner MR.
    Biochemistry; 2005 Jan 11; 44(1):82-96. PubMed ID: 15628848
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  • 14. Variation of Ser-L223 hydrogen bonding with the QB redox state in reaction centers from Rhodobacter sphaeroides.
    Ishikita H, Knapp EW.
    J Am Chem Soc; 2004 Jun 30; 126(25):8059-64. PubMed ID: 15212556
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  • 17. X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways.
    Xu Q, Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G.
    Structure; 2004 Apr 30; 12(4):703-15. PubMed ID: 15062092
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  • 18. Proton uptake by carboxylic acid groups upon photoreduction of the secondary quinone (QB) in bacterial reaction centers from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173.
    Nabedryk E, Breton J, Okamura MY, Paddock ML.
    Biochemistry; 1998 Oct 13; 37(41):14457-62. PubMed ID: 9772172
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  • 19. Protein/lipid interaction in the bacterial photosynthetic reaction center: phosphatidylcholine and phosphatidylglycerol modify the free energy levels of the quinones.
    Nagy L, Milano F, Dorogi M, Agostiano A, Laczkó G, Szebényi K, Váró G, Trotta M, Maróti P.
    Biochemistry; 2004 Oct 12; 43(40):12913-23. PubMed ID: 15461464
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  • 20. An isotope-edited FTIR investigation of the role of Ser-L223 in binding quinone (QB) and semiquinone (QB-) in the reaction center from Rhodobacter sphaeroides.
    Nabedryk E, Paddock ML, Okamura MY, Breton J.
    Biochemistry; 2005 Nov 08; 44(44):14519-27. PubMed ID: 16262252
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