Mutants of green fluorescent protein (GFP) have been used as biosensors for many purposes, including the monitoring of temperature, pH, and metal binding capabilities. While GFP does not show appreciable metal binding abilities, mutants of blue fluorescent protein (BFP) can bind copper, zinc, and possibly other metal ions effectively. Protein binding of these ions is typically monitored using fluorescence techniques, as the binding of metal ions to BFP mutants appreciably changes the observed fluorescence. In this work, further fluorescence characterization of metal binding by BFP is carried out using the recently developed polarized resonance synchronous spectroscopy (PRS2) technique combined with traditional fluorescence methods. PRS2 allows for the separation of the fluorophore on-resonance fluorescence (ORF), which is the photon emission at the same wavelength as the excitation photon, and light scattering. This technique could be further applied to monitor the movement of metal ions in living cells.

Analysis of metal binding in blue fluorescent protein using polarized resonance synchronous spectroscopy

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