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822 related items for PubMed ID: 21090818

  • 1. Electron-nuclear and electron-electron double resonance spectroscopies show that the primary quinone acceptor QA in reaction centers from photosynthetic bacteria Rhodobacter sphaeroides remains in the same orientation upon light-induced reduction.
    Flores M, Savitsky A, Paddock ML, Abresch EC, Dubinskii AA, Okamura MY, Lubitz W, Möbius K.
    J Phys Chem B; 2010 Dec 23; 114(50):16894-901. PubMed ID: 21090818
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  • 4. Low-temperature interquinone electron transfer in photosynthetic reaction centers from Rhodobacter sphaeroides and Blastochloris viridis: characterization of Q(B)- states by high-frequency electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR).
    Utschig LM, Thurnauer MC, Tiede DM, Poluektov OG.
    Biochemistry; 2005 Nov 01; 44(43):14131-42. PubMed ID: 16245929
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  • 5. Orientation-resolving pulsed electron dipolar high-field EPR spectroscopy on disordered solids: I. Structure of spin-correlated radical pairs in bacterial photosynthetic reaction centers.
    Savitsky A, Dubinskii AA, Flores M, Lubitz W, Möbius K.
    J Phys Chem B; 2007 Jun 07; 111(22):6245-62. PubMed ID: 17497913
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  • 6. 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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  • 8. QA binding in reaction centers of the photosynthetic purple bacterium Rhodobacter sphaeroides R26 investigated with electron spin polarization spectroscopy.
    van den Brink JS, Hulsebosch RJ, Gast P, Hore PJ, Hoff AJ.
    Biochemistry; 1994 Nov 22; 33(46):13668-77. PubMed ID: 7947775
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  • 10. Electron transfer pathways and protein response to charge separation in photosynthetic reaction centers: time-resolved high-field ENDOR of the spin-correlated radical pair P865(+)QA(-).
    Poluektov OG, Utschig LM, Dubinskij AA, Thurnauer MC.
    J Am Chem Soc; 2005 Mar 23; 127(11):4049-59. PubMed ID: 15771542
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  • 11. Conformation-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides.
    Kálmán L, Maróti P.
    Biochemistry; 1997 Dec 09; 36(49):15269-76. PubMed ID: 9398255
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  • 12. Steady-state FTIR spectra of the photoreduction of QA and QB in Rhodobacter sphaeroides reaction centers provide evidence against the presence of a proposed transient electron acceptor X between the two quinones.
    Breton J.
    Biochemistry; 2007 Apr 17; 46(15):4459-65. PubMed ID: 17381130
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  • 14. Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor.
    Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L.
    Biochemistry; 2011 Jun 14; 50(23):5249-62. PubMed ID: 21561160
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  • 15. Evidence for delocalized anticooperative flash induced proton binding as revealed by mutants at the M266His iron ligand in bacterial reaction centers.
    Cheap H, Tandori J, Derrien V, Benoit M, de Oliveira P, Koepke J, Lavergne J, Maroti P, Sebban P.
    Biochemistry; 2007 Apr 17; 46(15):4510-21. PubMed ID: 17378585
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  • 18. Electron paramagnetic resonance investigation of photosynthetic reaction centers from Rhodobacter sphaeroides R-26 in which Fe2+ was replaced by Cu2+. Determination of hyperfine interactions and exchange and dipole-dipole interactions between Cu2+ and QA-.
    Calvo R, Passeggi MC, Isaacson RA, Okamura MY, Feher G.
    Biophys J; 1990 Jul 17; 58(1):149-65. PubMed ID: 2166597
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