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Tuning the Selectivity and Reactivity of Metal‐Substituted Polyoxometalates as Artificial Proteases by Varying the Nature of the Embedded Lewis Acid Metal Ion
Author(s) -
Sap Annelies,
Van Tichelen Leentje,
Mortier Anneleen,
Proost Paul,
ParacVogt Tatja.
Publication year - 2016
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201601098
Subject(s) - chemistry , isostructural , selectivity , lewis acids and bases , hydrolysis , reactivity (psychology) , metal , cytochrome c , peptide bond , metal ions in aqueous solution , inorganic chemistry , medicinal chemistry , stereochemistry , peptide , organic chemistry , catalysis , crystal structure , medicine , biochemistry , alternative medicine , pathology , mitochondrion
The hydrolysis of horse heart cytochrome c (cytC) protein by two isostructural Keggin‐type polyoxometalates (POMs), (Me 2 NH 2 ) 10 [Ce(α‐PW 11 O 39 ) 2 ] (Ce1–K2) and (Et 2 NH 2 ) 10 [Zr(PW 11 O 39 ) 2 ] (Zr1–K2), which differ in the nature of the embedded Lewis acid metal ion, has been investigated. In the presence of Ce1–K2, selective hydrolysis of cytC was observed at the Trp60‐Lys61 and Gly78‐Thr79 peptide bonds at pH 7.4 and 37 °C. However, the isostructural Zr1–K2 exhibited a lower reactivity and different selectivity, cleaving cytC at the Asp3‐Val4, Asp51‐Ala52 and Gly78‐Thr79 peptide bonds. Different spectroscopic techniques were used to verify the molecular interactions between cytC and each metal‐substituted Keggin POM to elucidate the role of the Lewis acid metal ion in directing the selectivity of protein hydrolysis.