Fluoride activation of the cGMP cascade of vision requires the presence of aluminum, and is shown to be mediated by the binding of one AlF‐4 to the GDP/GTP‐binding subunit of transducin. The presence of GDP in the site is required: AlF4
− is ineffective when the site is empty or when GDPßS is substituted for GDP. This sensitivity to the sulfur of GDPßS suggests that AlF4
− is in contact with the GDP. Striking structural similarities between AlF4
− and PO4
−1 lead us to propose that AlF4
− mimics the role of the γ‐phosphate of GTP.
Fluoride activation of the cGMP cascade of vision requires the presence of aluminum, and is shown to be mediated by the binding of one AlF‐4 to the GDP/GTP‐binding subunit of transducin. The presence of GDP in the site is required: AlF4
− is ineffective when the site is empty or when GDPßS is substituted for GDP. This sensitivity to the sulfur of GDPßS suggests that AlF4
− is in contact with the GDP. Striking structural similarities between AlF4
− and PO4
−1 lead us to propose that AlF4
− mimics the role of the γ‐phosphate of GTP.
“…Besides, some publications exist using nuclear magnetic resonance as analytical tool concerning AlF x O y -species in solution [55][56][57], in zeolites (dealumination process or fluorination) or other F containing solids on AlPO 4 /SAPO basis [9,27,[58][59][60][61][62][63]. But in the most cases no distinct assignment to certain species was set, which is in the case for amorphous compounds due to the observation of broad and/or overlapping signals.…”
“…Although the kinetics of the ligands' exchange for this particular case have not been studied, it is generally known that the ligands are labile. It is also known that fluoride ions are able to replace the solvating water molecules in Al(H20)63+,21 and thus fluoroaluminum complexes, such as [FA1(H,0)5]2+ and [Al-F,aq]-, exist in aqueous solution 22. The stability of fluoro complexes is not surprising.…”
Fluoride is known to inhibit the photodynamic activity of aluminium phthalocyanine in a variety of biological systems. In order to gain insight into this phenomenon, the effect of fluoride on the photophysical properties of free and albumin-bound chloroaluminum phthalocyanine sulfonate (AlPcSn) were studied. The association constant of NaF with AlPcSn in aqueous solution was measured as 500 +/- 20 M-1. This binding affects the photophysical properties of the dye: the absorption bands in the visible range are blue-shifted by 6-8 nm, and this effect is mirrored in the fluorescence emission spectrum. Human serum albumin significantly quenched the dye fluorescence independent of the presence of fluoride ion. The transient absorption spectrum of the excited dye triplet is unchanged by NaF, but the quantum yield for its generation is increased by 50%, with no decrease in its lifetime. Formation of fluoroaluminum phthalocyanine complexes was also observed in tetrabutylammonium fluoride-assisted solutions in wet acetonitrile. The fluoro-AlPcSn complex is a better photosensitizer for generation of singlet oxygen than the original dye-hydroxyl ion complex, as confirmed using the imidazole-N,N-dimethyl-4-nitrosoaniline method. On the other hand, the fluoro-AlPcSn complex exhibits an intense inhibitory effect on photohemolysis of red blood cells (RBC) even after the cells are washed to remove free dye and fluoride prior to irradiation, indicating that once the dye is attached to the cellular site, the fluoride ligand is no longer prone to displacement (by hydroxyl ion, for example). Nonetheless, it is clear from the spectroscopic data that the new fluoro complex is an efficient sensitizer for photooxidation.(ABSTRACT TRUNCATED AT 250 WORDS)
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