tailieunhanh - Báo cáo khoa học: Does different orientation of the methoxy groups of ubiquinone-10 in the reaction centre of Rhodobacter sphaeroides cause different binding at QA and QB?

The different roles of ubiquinone-10 (UQ10) at the primary and secondary quinone (QAand QB) binding sites ofRho-dobacter sphaeroidesR26 reaction centres are governed by the protein microenvironment. The 4C¼O carbonyl group of QAis unusually strongly hydrogen-bonded, in contrast to QB. This asymmetric binding seems to determine their dif-ferent functions. The asymmetric hydrogen-bonding at QA can be caused intrinsically by distortion of the methoxy groups or extrinsically by binding to specific amino-acid side groups. . | Eur. J. Biochem. 270 3603-3609 2003 FEBS 2003 doi Does different orientation of the methoxy groups of ubiquinone-10 in the reaction centre of Rhodobacter sphaeroides cause different binding at QA and QB Andre Remy1 Rutger B. Boers2 Tatiana Egorova-Zachernyuk2 Peter Gast3 Johan Lugtenburg2 and Klaus Gerwert1 1Lehrstuhl fur Biophysik Ruhr-Universitdt Bochum Germany 2Department of Chemistry Gorlaeus Laboratories Leiden University the Netherlands 3Department of Biophysics Huygens Laboratory Leiden University the Netherlands The different roles of ubiquinone-10 UQ10 at the primary and secondary quinone QA and QB binding sites of Rho-dobacter sphaeroides R26 reaction centres are governed by the protein microenvironment. The 4C O carbonyl group of Qa is unusually strongly hydrogen-bonded in contrast to QB. This asymmetric binding seems to determine their different functions. The asymmetric hydrogen-bonding at QA can be caused intrinsically by distortion of the methoxy groups or extrinsically by binding to specific amino-acid side groups. Different X-ray-based structural models show contradictory orientations of the methoxy groups and do not provide a clear picture. To elucidate if distortion of the methoxy groups induces this hydrogen-bonding their ring- C-O vibrations were assigned by use of site-specifically labelled 5-13C UQ10 and 6-13C UQ10 reconstituted at either the QA or the QB binding site. Two infrared bands at 1288 cm-1 and 1264 cm-1 were assigned to the methoxy vibrations. They did not shift in frequency at either the QA or Qb binding sites as compared with unbound UQ10. As the frequencies of these vibrations and their coupling are sensitive to the conformations of the methoxy groups different conformations of the C 5 and C 6 methoxy groups at the Qa and Qb binding sites can now be excluded. Both methoxy groups are oriented out of plane at QA and QB. Therefore hydrogen-bonding to His M219 combined with electrostatic interactions

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