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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)

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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.
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aminopeptidase, metalloenzyme, critical, methionine, relevance, ions, vitro, assays, cofactor, int, cover, angel, chem, metali, inhibitors, view, picture, binding, 232005
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