title: Mechanistic aspects of proton chain transfer in the green fluorescent protein. Part II. A comparison of minimal quantum chemical models.
abstract: In this paper we report the results of extensive quantum chemical reaction pathway calculations for the electronic ground state of several different cluster models that mimic the proton chain transfer path within the green fluorescent protein (GFP). Our principal objective is to establish the robustness with respect to variations in the model of our recent mechanistic inferences for the ground state proton chain transfer [S. Wang and S. C. Smith, J. Phys. Chem. B, 2006, 110, 5084]. Additionally, comparison of our ground state results with the excited state proton transfer (ESPT) study by Vendrell et al. [O. Vendrell, R. Gelabert, M. Moreno and J. M. Lluch, J. Am. Chem. Soc., 2006, 128, 3564] leads to the conclusion that the mechanism of proton chain transfer may be expected to be analogous in ground and excited states, principally because in both cases the loss of the chromophore's phenolic proton contributes strongly to the reaction coordinate only late in the reaction path.
authors.affiliation: Centre for Computational Molecular Science, The University of Queensland, Brisbane, QLD 4072, Australia.
authors.forename: Sufan
authors.initials: S
authors.lastname: Wang
authors.forename: Sean C
authors.initials: SC
authors.lastname: Smith
mesh_terms: D003198:Computer Simulation; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D010316:Particle Size; D010777:Photochemistry / Q000379:methods*; D011487:Protein Conformation; D011522:Protons; D011789:Quantum Theory
chemical_list: D011522:Protons; D049452:Green Fluorescent Proteins