Resolution of insitu Interaction Energies between Molecules and the Reaction Center QA Site: Implications for Electron Transfer Function
We are interested in identifying the features of the cofactor-protein interaction which allow quinones and other molecules to perform intraprotein electron transfer reactions when bound at the primary quinone, or QA, site of the photosynthetic reaction center protein (RC) of Rhodobacter sphaeroides R26. This requires quantitation of the energetic contributions of specific, non-bonded contacts between cofactor and protein, such as hydrogen bonds and other strong electrostatic interactions. The strengths of these interactions are highly sensitive to the charge state of the conjugate oxidized and reduced forms (see 1), and thus influence the free energy gap for the electron transfer reaction through modulation of the quinone in situ midpoint potential (Em).
KeywordsElectron Transfer Reaction Midpoint Potential Quinone Compound Hexane System Single Hydrogen Bonding
Unable to display preview. Download preview PDF.
- 2.Jencks, W.P. (1975) Adv. Enzvmol. 43, 219–410Google Scholar
- 3.Warncke, K. and Dutton, P.L. (1989) Proc. Natl. Acad. Sci., (submitted)Google Scholar
- 5.Gunner, M.R., Warncke, K., Braun, B.S., Bruce, J.M. and Dutton, P.L. (1989) Biochemistry (submitted)Google Scholar
- 9.Trebst, A., Donner, W. and Draeber, W. (1984) Z. Naturforsch. 39c, 405–411Google Scholar