Cover Picture Metal Ions as Cofactors for the Binding of Inhibitors to Methionine Aminopeptidase A Critical View of the Relevance of In Vitro Metalloenzyme Assays (Angew. Chem. Int. Ed. 232005)код для вставкиСкачать
Cover Picture Rolf Schiffmann, Andreas Heine, Gerhard Klebe, and Christian D. P. Klein* Metalloenzymes are often studied in the presence of unphysiologically high concentrations of metal ions. This situation may lead to artifacts in assays if the binding of an inhibitor is made possible through additional metal ions; such compounds would appear highly potent in vitro, but may not possess activity in vivo. In their Communication on page 3620 ff., C. D. P. Klein and co-workers describe this effect with the enzyme methionine aminopeptidase as an example. (Mouse image provided by the U.S. National Park Service.) Surface Chemistry of Membranes The interactions between neighboring membranes that lead to the formation of protein patterns perform important biological functions. In his Review on page 3524 ff. J. T. Groves discusses these processes through the use of model systems and measurement techniques. Chirality Transfer A small organic molecule can transfer chirality to a large polyoxometalate cluster. How this transfer occurs is reported by C. L. Hill and co-workers in their Communication on page 3540 ff. Reaction Mechanisms K. N. Houk and co-workers describe computational studies of the thermal rearrangement of 6-methylenebicyclo[3.2.0]hept-2-ene in their Communication on page 3548 ff. The results suggest a bifurcation of reaction trajectories which explains the product ratios observed.