Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaeroides R-26, and bovine heart mitochondria.
Britt RD, Sauer K, Klein MP, Knaff DB, Kriauciunas A, Yu CA, Yu L, Malkin R
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
Correlation of paramagnetic states and molecular structure in bacterial photosynthetic reaction centers: the symmetry of the primary electron donor in Rhodopseudomonas viridis and Rhodobacter sphaeroides R-26.
Norris JR, Budil DE, Gast P, Chang CH, el-Kabbani O, Schiffer M
N-terminal sequences of subunits L and M of the photosynthetic reaction centre from Rhodospirillum rubrum G-9+. Separation of the subunits by gel filtration on hydroxypropylated Sephadex G 100 in organic solvents.
The light-harvesting polypeptides of Rhodopseudomonas sphaeroides R-26.1. II. Conformational analyses by attenuated total reflection infrared spectroscopy and the possible molecular structure of the hydrophobic domain of the B 850 complex.
Theiler R, Zuber H
Hoppe Seylers Z Physiol Chem
Light saturation curves and quantum yields in reaction centers from photosynthetic bacteria.
Triplet state energy transfer between the primary donor and the carotenoid in Rhodobacter sphaeroides R-26.1 reaction centers exchanged with modified bacteriochlorophyll pigments and reconstituted with spheroidene.
Frank HA, Chynwat V, Posteraro A, Hartwich G, Simonin I, Scheer H
Triplet energy transfer between the primary donor and carotenoids in Rhodobacter sphaeroides R-26.1 reaction centers incorporated with spheroidene analogs having different extents of pi-electron conjugation.
Farhoosh R, Chynwat V, Gebhard R, Lugtenburg J, Frank HA
Control of the unidirectional topological orientation of a cross-linked complex composed of the bacterial photosynthetic reaction center and horse heart cytochrome c reconstituted into proteoliposomes.
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, Mobius K
Femtosecond spectroscopy of electron transfer in the reaction center of the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26: Direct electron transfer from the dimeric bacteriochlorophyll primary donor to the bacteriopheophytin acceptor with a time constant of 2.8 +/- 0.2 psec.
Martin JL, Breton J, Hoff AJ, Migus A, Antonetti A
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.
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
Triplet-minus-singlet absorbance difference spectra of reaction centers of Rhodopseudomonas sphaeroides R-26 in the temperature range 24-290 K measured by Magneto-Optical Difference Spectroscopy (MODS).
* These data were automatically processed and therefore are not curated
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