Effect of ionic strength on intra-protein electron transfer reactions: The case study of charge recombination within the bacterial reaction center.
It is a common believe that intra-protein electron transfer (ET) involving reactants and products that are overall electroneutral are not influenced by the ions of the surrounding solution. The results presented here show an electrostatic coupling between the ionic atmosphere surrounding a membrane protein (the reaction center (RC) from the photosynthetic bacterium Rhodobacter sphaeroides) and two very different intra-protein ET processes taking place within it. Specifically we have studied the effect of salt concentration on: i) the kinetics of the charge recombination between the reduced primary quinone acceptor QA(-) and the primary photoxidized donor P(+); ii) the thermodynamic equilibrium (QA(-)↔QB(-)) for the ET between QA(-) and the secondary quinone acceptor QB. A distinctive point of this investigation is that reactants and products are overall electroneutral. The protein electrostatics has been described adopting the lowest level of complexity sufficient to grasp the experimental phenomenology and the impact of salt on the relative free energy level of reactants and products has been evaluated according to suitable thermodynamic cycles. The ionic strength effect was found to be independent on the ion nature for P(+)QA(-) charge recombination where the leading electrostatic term was the dipole moment. In the case of the QA(-)↔QB(-) equilibrium, the relative stability of QA(-) and QB(-) was found to depend on the salt concentration in a fashion that is different for chaotropic and kosmotropic ions. In such a case both dipole moment and quadrupole moments of the RC must be considered.
Chemistry Department, University of Rome "La Sapienza", Italy; CSGI (Center for Colloid and Surface Science), c/o Dept. Chemistry, via Orabona 4, 70125 Bari, Italy. Electronic address: mauro.giustini@uniroma1.it.
Mauro
M
Giustini
Dutch Institute for Fundamental Energy Research (DIFFER), De Zaale 20, 5612, AJ, Eindhoven, The Netherlands.
Matteo
M
Parente
CNR-IPCF, Istituto per i processi chimico fisici, c/o Dept. Chemistry, via Orabona 4, 70125 Bari, Italy.
Antonia
A
Mallardi
Chemistry Department, University of Bari, via Orabona 4, 70125 Bari, Italy; CSGI (Center for Colloid and Surface Science), c/o Dept. Chemistry, via Orabona 4, 70125 Bari, Italy. Electronic address: gerardo.palazzo@uniba.it.
Gerardo
G
Palazzo
D004579:Electron Transport; D009994:Osmolar Concentration; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000378:metabolism*; D055672:Static Electricity; D013816:Thermodynamics
D045322:Photosynthetic Reaction Center Complex Proteins
Charge recombination; Hofmeister series, Debye screening length; Intra-protein electron transfer; Rhodobacter sphaeroides