No abstract

In order to make polyacrylonitrile (PAN) fluidic, acrylonitrile telomer (ANT) is synthesized by radical telomerization and used as a nitrogen and carbon precursor to prepare a non-noble oxygen reduction reaction (ORR) catalyst. This fluidic precursor greatly increases the contact between Fe salt aggregates and the polymer so that more active sites are formed during stabilization and carbonization. Such prepared catalysts and the commercial Pt/C catalyst have comparable ORR performance and stability.

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Drosophila 14-3-3 (D14-3-3) modulates the activity of the Slowpoke calcium-dependent potassium channel (dSlo) by interacting with the dSlo binding protein, Slob. We show here that D14-3-3 forms dimers in vitro. Site-directed mutations in its putative dimerization interface result in a dimerization-deficient form of D14-3-3. Both the wild-type and dimerization-deficient forms of D14-3-3 bind to Slob with similar affinity and form complexes with dSlo. When dSlo and Slob are expressed in mammalian cells, the dSlo channel activity is similarly modulated by co-expression of either the wild-type or the dimerization-deficient form of D14-3-3. In addition, dSlo is still modulated by wild-type D14-3-3 in the presence of a 14-3-3 mutant, which does not itself bind to Slob but forms heterodimers with the wild-type 14-3-3. These data, taken together, suggest that monomeric D14-3-3 is capable of modulating dSlo channel activity in this regulatory complex.