The bacterial photosynthetic reaction center (RC) of Rhodobacter sphaeroides is a protein-pigment complex capable of photosynthesis, a process that converts light energy into chemical energy by a chain of photoinduced electron transfer (ET) reactions. [1,2] Recent studies suggest that the reaction center can be used for the construction of new efficient bioinorganic photovoltaic devices converting solar energy into electricity or chemical energy. [3][4][5][6][7] The efficiency of enzyme-based bioinorganic devices critically depends on the rate of electron transfer between the electrode and the protein. Recently, we demonstrated that ET from the flat gold electrode to the immobilized RC increases by several orders of magnitude when one incorporates between them cytochrome c, a natural photosynthetic electron transfer mediator. [7] One of the possible explanations of this effect is that cytochrome penetrates efficiently into RC and thus improves electron coupling between the protein and the electrode. If this is true, then it is possible that optimizing the shape of the electrode itself could improve the conductivity of the RC-electrode interface even without cytochrome. To evaluate this possibility herein, we calculate the efficiency of the ET (electron matrix coupling element) between the electrode and the RC when cytochrome c is replaced with metal nanoparticles of various diameters.For these calculations, we develop a new approach based on recent advances in the theory of molecular electron transfer and optimization theory. It is based on the shortest path algorithm that incorporates the pathway model of Beratan and Onuchic, [8] developed to estimate the ET rates in proteins. In addition, our approach considers the electronic tunneling through water and incorporates the possibility of a simultaneous ET to any part of a larger partner such as a metal nanocluster.In our calculations, the gold nanocluster was assumed to have an Fm3m group symmetry (space group number 225), the atomic coordinates for the RC were obtained from the Protein Database (http://www.rcsb.org/pdb/, file "1PCR''), and the structure of RC-nanocluster complexes was optimized by minimization of the electrostatic potential energy calculated as the result of induced charge distribution on the nanoparticle under the constraints that do not allow the overlapping of the van der Waals surfaces of the protein and the nanoparticle. We approximate the metal nanoparticles by fitting geometrical spheres of various radii and consider the flat surface as a plane. The smallest possible distance R 0 between protein and the nanoparticle was taken as R 0 ¼ 0:286 nm, which is equal to the sum of the van der Waals radii of a hydrogen atom belonging to surface of the RC and an atom of gold. We have chosen water to be the surrounding medium. The calculation of the positions of the metal relative to the RC shows that the shortest distance between the metal cluster and the protein special pair is about 1 nm ( Figure 1). This distance is similar to the distance betwee...