AutoriSrinivasan N, Santabarbara S, Rappaport F, Carbonera D, Redding K, van der Est A, Golbeck JH.
AbstractIn Photosystem I, the backbone nitrogen of Leu722(PsaA) forms a hydro-gen bond with the C(4) carbonyl oxygen of phylloquinone in the A(1A) site. A previous low-temperature EPR study indicated that substitution of Leu722(PsaA) with a bulky Trp residue results in a weakened H-bond. Here, we employ room temperature, time-resolved optical spectroscopy and variable temperature, transient EPR spectroscopy to probe the effect of the altered H-bond on the energetics and kinetics of electron transfer. Relative to the wild type, we find that the rate of electron transfer from A(1A)(-) to F(X) in the L722W(PsaA) variant is faster by a factor of 3. This change is attributed to a lowered midpoint potential of A(1A)/A(1A)(-), resulting in a larger Gibbs free energy change between A(1A)/A(1A)(-) and F(X)/F(X)(-). An activation energy of 180±10 meV is determined for the A(1A)(-)-to-F(X) forward electron transfer step in the L722W(PsaA) variant compared with 220±10 meV in the wild type. The Arrhenius plot shows a break at ~200 K, below which the rate becomes nearly independent of temperature. This behavior is described using a quantum mechanical treatment that takes the zero-point energy into account as well as an alternative model that invokes a dynamical transition in the protein at ~200 K.
RivistaThe Journal Of Physical Chemistry. B
Impact factor0
Pagina inizio1751
Pagina fine1759.
Linee di Ricerca IBFMD.P01.005.001