BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

376 related articles for article (PubMed ID: 10512634)

  • 1. 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; 38(36):11773-87. PubMed ID: 10512634
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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; 40(20):6132-41. PubMed ID: 11352751
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 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; 44(43):14131-42. PubMed ID: 16245929
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 39(11):2961-9. PubMed ID: 10715116
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 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; 129(51):15935-46. PubMed ID: 18052250
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Protein-cofactor interactions in bacterial reaction centers from Rhodobacter sphaeroides R-26: II. Geometry of the hydrogen bonds to the primary quinone formula by 1H and 2H ENDOR spectroscopy.
    Flores M; Isaacson R; Abresch E; Calvo R; Lubitz W; Feher G
    Biophys J; 2007 Jan; 92(2):671-82. PubMed ID: 17071655
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 114(50):16894-901. PubMed ID: 21090818
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 114(45):14364-72. PubMed ID: 20345158
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Protein-cofactor interactions in bacterial reaction centers from Rhodobacter sphaeroides R-26: effect of hydrogen bonding on the electronic and geometric structure of the primary quinone. A density functional theory study.
    Sinnecker S; Flores M; Lubitz W
    Phys Chem Chem Phys; 2006 Dec; 8(48):5659-70. PubMed ID: 17149487
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The conformation of the isoprenyl chain relative to the semiquinone head in the primary electron acceptor (QA) of higher plant PSII (plastosemiquinone) differs from that in bacterial reaction centers (ubisemiquinone or menasemiquinone) by ca. 90 degrees.
    Zheng M; Dismukes GC
    Biochemistry; 1996 Jul; 35(27):8955-63. PubMed ID: 8688432
    [TBL] [Abstract][Full Text] [Related]  

  • 12. EPR and ENDOR investigation of the primary electron acceptor radical anion QA.- in iron-depleted photosystem II membrane fragments.
    MacMillan F; Lendzian F; Renger G; Lubitz W
    Biochemistry; 1995 Jun; 34(25):8144-56. PubMed ID: 7794928
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Efficient exchange of the primary quinone acceptor Q(A) in isolated reaction centers of Rhodopseudomonas viridis.
    Breton J
    Proc Natl Acad Sci U S A; 1997 Oct; 94(21):11318-23. PubMed ID: 11038584
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Effects of copper and zinc ions on photosystem II studied by EPR spectroscopy.
    Jegerschöld C; MacMillan F; Lubitz W; Rutherford AW
    Biochemistry; 1999 Sep; 38(38):12439-45. PubMed ID: 10493813
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Asymmetric binding of the primary acceptor quinone in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides R26, probed with Q-band (35 GHz) EPR spectroscopy.
    van den Brink JS; Spoyalov AP; Gast P; van Liemt WB; Raap J; Lugtenburg J; Hoff AJ
    FEBS Lett; 1994 Oct; 353(3):273-6. PubMed ID: 7957873
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Electronic structure of Q-A in reaction centers from Rhodobacter sphaeroides. I. Electron paramagnetic resonance in single crystals.
    Isaacson RA; Lendzian F; Abresch EC; Lubitz W; Feher G
    Biophys J; 1995 Aug; 69(2):311-22. PubMed ID: 8527644
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Hyperfine and nuclear quadrupole tensors of nitrogen donors in the Q(A) site of bacterial reaction centers: correlation of the histidine N(δ) tensors with hydrogen bond strength.
    Taguchi AT; O'Malley PJ; Wraight CA; Dikanov SA
    J Phys Chem B; 2014 Aug; 118(31):9225-37. PubMed ID: 25026433
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Proton uptake associated with the reduction of the primary quinone Q(A) influences the binding site of the secondary quinone Q(B) in Rhodopseudomonas viridis photosynthetic reaction centers.
    Zachariae U; Lancaster CR
    Biochim Biophys Acta; 2001 Jun; 1505(2-3):280-90. PubMed ID: 11334792
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Probing subtle coordination changes in the iron-quinone complex of photosystem II during charge separation, by the use of NO.
    Goussias C; Deligiannakis Y; Sanakis Y; Ioannidis N; Petrouleas V
    Biochemistry; 2002 Dec; 41(51):15212-23. PubMed ID: 12484759
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Hydrogen bonding and spin density distribution in the Qb semiquinone of bacterial reaction centers and comparison with the Qa site.
    Martin E; Samoilova RI; Narasimhulu KV; Lin TJ; O'Malley PJ; Wraight CA; Dikanov SA
    J Am Chem Soc; 2011 Apr; 133(14):5525-37. PubMed ID: 21417328
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 19.