Angewandte Chemie International Edition
© WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Cover Picture: Observation of the Fe-CN and Fe-CO Vibrations in the Active Site of [NiFe] Hydrogenase by Nuclear Resonance Vibrational Spectroscopy (Angew. Chem. Int. Ed. 2/2013)
The active site of [NiFe] hydrogenase is an excellent catalyst for hydrogen conversion with an intriguing ability to recover from exposure to dioxygen. In their Communication on page 724 ff., W. Lubitz, S. P. Cramer, and co-workers use the synchrotron technique of nuclear resonance vibrational spectroscopy to identify normal modes associated with active-site Fe-CN and Fe-CO motion.
Also of Interest
H. A. Lashuel and co-workers show in their Communication on page 562 ff. that an N-terminal domain in the huntingtin protein is highly prone to aggregation. The consequences for toxicity are discussed.
An approach for predicting residual dipolar couplings from disordered protein chains is reported by M. Blackledge et al. in their Communication on page 687 ff.
In their Communication on page 645 ff., A. W. Xu et al. describe the synthesis of highly branched star-shaped bimetallic nanocrystals and their application as catalysts for the oxidation of ethanol.