title: Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix.
abstract: Many proteins can be immobilized in silica hydrogel matrices without compromising their function, making this a suitable technique for biosensor applications. Immobilization will in general affect protein structure and dynamics. To study these effects, we have measured the P(+)Q(A)(-) charge recombination kinetics after laser excitation of Q(B)-depleted wild-type photosynthetic reaction centers from Rhodobacter sphaeroides in a tetramethoxysilane (TMOS) sol-gel matrix and, for comparison, also in cryosolvent. The nonexponential electron transfer kinetics observed between 10 and 300 K were analyzed quantitatively using the spin boson model for the intrinsic temperature dependence of the electron transfer and an adiabatic change of the energy gap and electronic coupling caused by protein motions in response to the altered charge distributions. The analysis reveals similarities and differences in the TMOS-matrix and bulk-solvent samples. In both preparations, electron transfer is coupled to the same spectrum of low frequency phonons. As in bulk solvent, charge-solvating protein motions are present in the TMOS matrix. Large-scale conformational changes are arrested in the hydrogel, as evident from the nonexponential kinetics even at room temperature. The altered dynamics is likely responsible for the observed changes in the electronic coupling matrix element.
authors.affiliation: Department of Biophysics, University of Ulm, Ulm, Germany.
authors.forename: Jan M
authors.initials: JM
authors.lastname: Kriegl
authors.forename: Florian K
authors.initials: FK
authors.lastname: Forster
authors.forename: G Ulrich
authors.initials: GU
authors.lastname: Nienhaus
mesh_terms: D004583:Electrons; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate / Q000737:chemistry; D007700:Kinetics; D008027:Light; D008956:Models, Chemical; D008962:Models, Theoretical; D044367:Phase Transition; D010788:Photosynthesis / Q000502:physiology*; D045322:Photosynthetic Reaction Center Complex Proteins; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D011995:Recombination, Genetic; D012242:Rhodobacter sphaeroides / Q000378:metabolism; D012821:Silanes / Q000737:chemistry; D013053:Spectrophotometry; D013696:Temperature; D013997:Time Factors
chemical_list: D045322:Photosynthetic Reaction Center Complex Proteins; D011506:Proteins; D012821:Silanes; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate; C061205:tetramethoxysilane; C071717:trimethoxysilane