Abstract
Abstract Ten proteins that exhibit long-lived phosphorescence lifetimes at room temperature were examined for sensitivity to quenching by molecules that are external to the protein. The bimolecular quenching rate constant was found to decrease exponentially with the distance of the tryptophan from the protein surface. Theoretical analysis shows that this behavior is expected for an electron-exchange reaction between the buried tryptophan and quenchers in solution in the rapid diffusion limit. The results allow evaluation of the distance parameter, ρ, for electron transfer through the general protein matrix at 1.0 A, For a unimolecular donor-acceptor pair with ket = ko exp(-r/ρ), ko = 109sec−1.
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