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A new one-step synthetic protocol of tris-functionalized Anderson polyoxomolybdates directly from heptamolybdate salts was presented in this Communication. Through this new method, we obtained the first example of Anderson-type polyoxomolybdates with vanadium as the heteroatom. Moreover, the crystals of the products exhibited interesting nanocage or framework extended structures, which were greatly affected by the trialkoxyl ligands as well as the counterions.

The main light-activated enzyme of the vertebrate photoreceptor is cGMP phosphodiesterase, whose product is GMP. GMP would be broken down to guanosine by the enzyme 5'-nucleotidase on the cytoplasmic (extradiscal) surface of the disks. The presence of 5'-nucleotidase on the cytoplasmic surface was verified by using sucrose continuous gradients to show its association with the photoreceptors and by using disk preparation and concanavalin A binding to demonstrate its presence on the extradiscal surface. Further studies using detergents and freeze-thaw showed that an even higher 5'-nucleotidase activity is present on the intradiscal surface; however, it is the smaller cytoplasmic surface activity that is potentially relevant to the physiology. The 5'-nucleotidase on the extradiscal surface is light insensitive, has a broad optimal pH range, shows a divalent cation dependence, and is competitively inhibited by nucleoside di- and triphosphates. When the data determined experimentally were extrapolated to physiological conditions, we obtained a decay time constant for GMP breakdown by 5'-nucleotidase in the range of 0.4 to 1.06 s. This time constant is in the range of the time constants of the fall of rod cell receptor potential, suggesting a possible role for GMP level in visual transduction.

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