What is it about?

Proteins sharing the same “2-His-1-carboxylate” structural motif have little amino acid sequence similarity and are able to perform many different reactions. Many factors have been cited to explain their different specificity and turnover rates, like protein environment, coordinated ligand geometry, electronic structure of the active site, etc. This paper presents combined approach applying high-resolution XANES spectroscopy and theory simulations to different model complexes that mimic the binding modes of the amino acids to the metal site.

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Why is it important?

This study shows the subtle correlation between the orientation of the carboxylate and the absorption edge features.

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This page is a summary of: Kβ Detected High‐Resolution XANES of FeII and FeIII Models of the 2‐His‐1‐Carboxylate Motif: Analysis of the Carboxylate Binding Mode, European Journal of Inorganic Chemistry, January 2012, Wiley,
DOI: 10.1002/ejic.201101075.
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