Classical master equation for excitonic transport under the influence of an environment.
In a previous paper [Phys. Rev. E 83, 051911 (2011)] we have shown that the results of a quantum-mechanical calculation of electronic energy transfer (EET) over aggregates of coupled monomers can be described also by a model of interacting classical electric dipoles in a weak-coupling approximation, which we referred to as the realistic coupling approximation (RCA). The method was illustrated by EET on a simple linear chain of molecules and also by energy transfer on an arrangement of monomers corresponding to that of the Fenna-Matthews-Olson (FMO) complex relevant for photosynthesis. The study was limited to electronic degrees of freedom, since this is the origin of coherent EET in the quantum case. Nevertheless, more realistic models of EET require the inclusion of the decohering effects of coupling to an environment, when the molecular aggregate becomes an open quantum system. Here we consider the quantum description of EET on a linear chain and on the FMO complex, incorporating environment coupling and constructing the classical version of the same systems in the density matrix formalism. The close agreement of the exact quantum and exact classical results in the RCA is demonstrated and justified analytically in the RCA. This lends further support to the conclusion that the coherence properties of EET in the FMO complex are evident at the classical level and should not be ascribed as solely due to quantum effects.
Max Planck Institute for the Physics of Complex Systems, Dresden, Germany. eisfeld@mpipks-dresden.mpg.de
Alexander
A
Eisfeld
John S
JS
Briggs
D000465:Algorithms; D001703:Biophysics / Q000379:methods*; D004579:Electron Transport; D004583:Electrons; D004735:Energy Transfer; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism; D008390:Markov Chains; D015233:Models, Statistical; D009991:Oscillometry / Q000379:methods; D010788:Photosynthesis; D011336:Probability; D011789:Quantum Theory
D045342:Light-Harvesting Protein Complexes