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1389 related items for PubMed ID: 2166597

  • 1. 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; 58(1):149-65. PubMed ID: 2166597
    [Abstract] [Full Text] [Related]

  • 2. EPR investigation of Cu2+-substituted photosynthetic bacterial reaction centers: evidence for histidine ligation at the surface metal site.
    Utschig LM, Poluektov O, Tiede DM, Thurnauer MC.
    Biochemistry; 2000 Mar 21; 39(11):2961-9. PubMed ID: 10715116
    [Abstract] [Full Text] [Related]

  • 3. Cu2+ site in photosynthetic bacterial reaction centers from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodopseudomonas viridis.
    Utschig LM, Poluektov O, Schlesselman SL, Thurnauer MC, Tiede DM.
    Biochemistry; 2001 May 22; 40(20):6132-41. PubMed ID: 11352751
    [Abstract] [Full Text] [Related]

  • 4. Iron-depleted reaction centers from Rhodopseudomonas sphaeroides R-26.1: characterization and reconstitution with Fe2+, Mn2+, Co2+, Ni2+, Cu2+, and Zn2+.
    Debus RJ, Feher G, Okamura MY.
    Biochemistry; 1986 Apr 22; 25(8):2276-87. PubMed ID: 3011083
    [Abstract] [Full Text] [Related]

  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. Electron paramagnetic resonance studies of zinc-substituted reaction centers from Rhodopseudomonas viridis.
    Gardiner AT, Zech SG, MacMillan F, Käss H, Bittl R, Schlodder E, Lendzian F, Lubitz W.
    Biochemistry; 1999 Sep 07; 38(36):11773-87. PubMed ID: 10512634
    [Abstract] [Full Text] [Related]

  • 7. 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
    [Abstract] [Full Text] [Related]

  • 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
    [Abstract] [Full Text] [Related]

  • 9. Structure of the charge separated state P865(+)Q(A)- in the photosynthetic reaction centers of Rhodobacter sphaeroides by quantum beat oscillations and high-field electron paramagnetic resonance: evidence for light-induced Q(A)- reorientation.
    Heinen U, Utschig LM, Poluektov OG, Link G, Ohmes E, Kothe G.
    J Am Chem Soc; 2007 Dec 26; 129(51):15935-46. PubMed ID: 18052250
    [Abstract] [Full Text] [Related]

  • 10. Influence of iron-removal procedures on sequential electron transfer in photosynthetic bacterial reaction centers studied by transient EPR spectroscopy.
    Utschig LM, Greenfield SR, Tang J, Laible PD, Thurnauer MC.
    Biochemistry; 1997 Jul 15; 36(28):8548-58. PubMed ID: 9214300
    [Abstract] [Full Text] [Related]

  • 11. Electrostatic influence of QA reduction on the IR vibrational mode of the 10a-ester C==O of HA demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides.
    Breton J, Nabedryk E, Allen JP, Williams JC.
    Biochemistry; 1997 Apr 15; 36(15):4515-25. PubMed ID: 9109660
    [Abstract] [Full Text] [Related]

  • 12. Coupling of electron transfer to proton uptake at the Q(B) site of the bacterial reaction center: a perspective from FTIR difference spectroscopy.
    Nabedryk E, Breton J.
    Biochim Biophys Acta; 2008 Oct 15; 1777(10):1229-48. PubMed ID: 18671937
    [Abstract] [Full Text] [Related]

  • 13. Bacterial photosynthetic reaction centers in trehalose glasses: coupling between protein conformational dynamics and electron-transfer kinetics as studied by laser-flash and high-field EPR spectroscopies.
    Savitsky A, Malferrari M, Francia F, Venturoli G, Möbius K.
    J Phys Chem B; 2010 Oct 07; 114(39):12729-43. PubMed ID: 20839819
    [Abstract] [Full Text] [Related]

  • 14. The electronic structure of Fe2+ in reaction centers from Rhodopseudomonas sphaeroides. III. EPR measurements of the reduced acceptor complex.
    Butler WF, Calvo R, Fredkin DR, Isaacson RA, Okamura MY, Feher G.
    Biophys J; 1984 May 07; 45(5):947-73. PubMed ID: 6329347
    [Abstract] [Full Text] [Related]

  • 15. 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
    [Abstract] [Full Text] [Related]

  • 16. B-branch electron transfer in the photosynthetic reaction center of a Rhodobacter sphaeroides quadruple mutant. Q- and W-band electron paramagnetic resonance studies of triplet and radical-pair cofactor states.
    Marchanka A, Savitsky A, Lubitz W, Möbius K, van Gastel M.
    J Phys Chem B; 2010 Nov 18; 114(45):14364-72. PubMed ID: 20345158
    [Abstract] [Full Text] [Related]

  • 17. Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.
    Allen JP, Feher G, Yeates TO, Komiya H, Rees DC.
    Proc Natl Acad Sci U S A; 1988 Nov 18; 85(22):8487-91. PubMed ID: 3054889
    [Abstract] [Full Text] [Related]

  • 18. Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212-->Gln mutant reaction centers from Rhodobacter sphaeroides.
    McPherson PH, Schönfeld M, Paddock ML, Okamura MY, Feher G.
    Biochemistry; 1994 Feb 08; 33(5):1181-93. PubMed ID: 8110749
    [Abstract] [Full Text] [Related]

  • 19. Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: dynamics of binding and interaction upon QA and QB reduction.
    Hienerwadel R, Thibodeau D, Lenz F, Nabedryk E, Breton J, Kreutz W, Mäntele W.
    Biochemistry; 1992 Jun 30; 31(25):5799-808. PubMed ID: 1610825
    [Abstract] [Full Text] [Related]

  • 20. 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
    [Abstract] [Full Text] [Related]

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