Amino acid protonation states determine binding sites of the secondary ubiquinone and its anion in the Rhodobacter sphaeroides photosynthetic reaction center
- Univ. of Oklahoma, Norman, OK (United States). Dept. of Chemistry and Biochemistry
Molecular dynamics simulations of native ubiquinone-10 binding in the photosynthetic reaction center of Rhodobacter sphaeroides are presented that support the theory that the neutral and radical anionic quinones Q{sub B} and Q{sub B}{sup {sm_bullet}{minus}} bind in different locations. The differences in binding are attributed to differing protonation states of the nearby amino acids GLU L212 and ASP L213. Q{sub B} binding at the dark-adapted Q{sub B} site observed by Stowell et al. is most consistent with protonation of GLU L212. Q{sub B}{sup {sm_bullet}{minus}} binding at the experimentally observed light-adapted Q{sub B}{sup {sm_bullet}{minus}} site is consistent only with protonation of both GLU L212 and ASP L213. The experimentally established pH dependence of electron-transfer rate, combined with the MD results, implies that protonation of ASP L213 must occur before electron transfer. Additionally, the molecular dynamics results suggest that movement of the semiquinone anion Q{sub B}{sup {sm_bullet}} between sites (for different amino acid protonation states) is spontaneous near room temperature and cannot be itself account for the higher of two experimentally observed activation energies for electron transfer from Q{sub A} to Q{sub B}.
- Sponsoring Organization:
- USDOE Office of Energy Research, Washington, DC (United States)
- DOE Contract Number:
- FG03-97ER14806
- OSTI ID:
- 682106
- Journal Information:
- Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical, Vol. 103, Issue 25; Other Information: PBD: 24 Jun 1999
- Country of Publication:
- United States
- Language:
- English
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