0000000000089754
AUTHOR
Francesco Francia
Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrices.
Abstract The coupling between electron transfer and protein dynamics has been studied in photosynthetic reaction centers (RC) from Rhodobacter sphaeroides by embedding the protein into room temperature solid trehalose–water matrices. Electron transfer kinetics from the primary quinone acceptor (Q A − ) to the photoxidized donor (P + ) were measured as a function of the duration of photoexcitation from 20 ns (laser flash) to more than 1 min. Decreasing the water content of the matrix down to ≈5×10 3 water molecules per RC causes a reversible four-times acceleration of P + Q A − recombination after the laser pulse. By comparing the broadly distributed kinetics observed under these conditions …
Cytochrome c in a Dry Trehalose Matrix: Structural and Dynamical Effects Probed by X-Ray Absorption Spectroscopy
AbstractWe report on the structure and dynamics of the Fe ligand cluster of reduced horse heart cytochrome c in solution, in a dried polyvinyl alcohol (PVA) film, and in two trehalose matrices characterized by different contents of residual water. The effect of the solvent/matrix environment was studied at room temperature using Fe K-edge x-ray absorption fine structure (XAFS) spectroscopy. XAFS data were analyzed by combining ab initio simulations and multi-parameter fitting in an attempt to disentangle structural from disorder parameters. Essentially the same structural and disorder parameters account adequately for the XAFS spectra measured in solution, both in the absence and in the pre…