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Cover Picture: Protein Surface Mimetics: Understanding How Ruthenium Tris(Bipyridines) Interact with Proteins (ChemBioChem 2/2017)
Author(s) -
Hewitt Sarah H.,
Filby Maria H.,
Hayes Ed,
Kuhn Lars T.,
Kalverda Arnout P.,
Webb Michael E.,
Wilson Andrew J.
Publication year - 2017
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.201600683
Subject(s) - ruthenium , chemistry , tris , stereochemistry , cytochrome , cytochrome c , combinatorial chemistry , organic chemistry , biochemistry , enzyme , mitochondrion , catalysis
The cover picture shows competitive inhibition of the cytochrome c /cytochrome c peroxidase interaction by highly functionalized ruthenium(II) tris(bipyridine) complexes. Inhibition is achieved through recognition of the solvent‐exposed surface of cytochrome c using ruthenium(II) tris(bipyridine) complexes at the cytochrome c peroxidase binding site, as shown by 950 MHz natural‐abundance NMR spectroscopy and detailed fluorescence studies. Binding is driven by entropy and electrostatic effects with additional potency arising in higher‐affinity complexes from enthalpic contributions. More information can be found in the full paper by A. J. Wilson et al. page 223 in Issue 2, 2017 (DOI: 10.1002/cbic.201600552).