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.
The reaction center (RC)-bound primary acceptor quinone QA of the photosynthetic bacterium Rhodobacter sphaeroides R26 functions as a one-electron gate. The radical anion QA.- is proposed to have an asymmetric electron distribution, induced by the protein environment. We replace the native ubiquinone-10 (UQ10) with specifically 13C-labelled UQ10, and use Q-band (35 GHz) EPR spectroscopy to investigate this phenomenon in closer detail. The direct observation of the 13C-hyperfine splitting of the gz-component of UQ10A.- in the RC and in frozen isopropanol shows that the electron spin distribution is symmetric in the isopropanol glass, and asymmetric in the RC. Our results allow qualitative assessment of the spin and charge distribution for QA.- in the RC. The carbonyl oxygen of the semiquinone anion nearest to the S = 2 Fe(2+)-ion and QB is shown to acquire the highest (negative) charge density.
Department of Biophysics, Huygens Laboratory, Leiden University, The Netherlands.
J S
JS
van den Brink
A P
AP
Spoyalov
P
P
Gast
W B
WB
van Liemt
J
J
Raap
J
J
Lugtenburg
A J
AJ
Hoff
D000433:1-Propanol; D000838:Anions / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods; D015394:Molecular Structure; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D014451:Ubiquinone / Q000737:chemistry*
D000838:Anions; D045322:Photosynthetic Reaction Center Complex Proteins; D014451:Ubiquinone; D000433:1-Propanol; C025204:Ubiquinone Q2