Amino Acid Protonation States Determine Binding Sites of the Secondary Ubiquinone and Its Anion in the Rhodobacter sphaeroides Photosynthetic Reaction Center
| Autor: | Ralph A. Wheeler, Anthony K. Grafton |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Photosynthetic reaction centre
chemistry.chemical_classification biology Stereochemistry Protonation biology.organism_classification Photochemistry Surfaces Coatings and Films Ion Amino acid Molecular dynamics Electron transfer Rhodobacter sphaeroides chemistry Materials Chemistry Physical and Theoretical Chemistry Binding site |
| Zdroj: | The Journal of Physical Chemistry B. 103:5380-5387 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/jp9901139 |
| Popis: | 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 QB and QB•- bind in different locations. The differences in binding are attributed to differing protonation states of the nearby amino acids GLU L212 and ASP L213. QB binding at the “dark-adapted” QB site observed by Stowell et al. is most consistent with protonation of GLU L212. QB•- binding at the experimentally observed “light-adapted” QB•- site is consistent only with protonation of both GLU L212 and ASP L213. The experimentally established pH dependence of electron-transfer rate, combined with our 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 QB•- between sites (for different amino acid protonation states) is spontaneous near room temperature and cannot by itself... |
| Databáze: | OpenAIRE |
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