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Cover Picture: Complex Gadolinium–Oxo Clusters Formed along Concave Protein Surfaces (ChemBioChem 15/2012)
Author(s) -
Veelders Maik,
Essen LarsOliver
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201290062
Subject(s) - gadolinium , chemistry , crystallography , lanthanide , cluster (spacecraft) , fragment crystallizable region , biochemistry , organic chemistry , ion , receptor , computer science , programming language
The cover picture shows the assembly of a complex gadolinium cluster (gold) along a unique, acidic surface patch of the yeast cell adhesion domain Flo5A that was formally identified as a secondary carbohydrate binding site. The step‐wise formation of this heptanuclear gadolinium complex in crystals of Flo5A mimics the nucleation and deposition of iron‐oxo clusters along ferritin surfaces. In the communication on p. 2187 ff., L.‐O. Essen and M. Veelders show that the complex's unprecedented composite structure, which consists of a distorted Gd 4 O 4 cubane and a trinuclear Gd 3 O 5 cluster, requires coordination to four aspartic acid residues of the protein. Incorporation of the gadolinium cluster on the protein surface depends on the early formation of μ‐oxo‐bridged lanthanide cores. The observation that aspartates suitably placed on protein surfaces foster gadolinium cluster formation constitutes a paradigm for protein‐based biohybrids carrying metallo‐oxo clusters. This could, in future, lead to the design of protein‐based templates for polynuclear gadolinium complexes and hence to site‐specific and biocompatible MRI contrast agents.