Premium
Phosphoester Hydrolysis: The Incoming Substrate Turns the Bridging Hydroxido Nucleophile into a Terminal One
Author(s) -
Gouré Eric,
Carboni Michaël,
Troussier Angélique,
Lebrun Colette,
Pécaut Jacques,
Jacquot JeanFrançois,
Dubourdeaux Patrick,
Clémancey Martin,
Blondin Geneviève,
Latour JeanMarc
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201500977
Subject(s) - nucleophile , hydrolysis , chemistry , hydroxide , phosphodiester bond , catalysis , substrate (aquarium) , ligand (biochemistry) , solvolysis , phosphate , stereochemistry , medicinal chemistry , inorganic chemistry , organic chemistry , rna , biochemistry , oceanography , receptor , gene , geology
Identifying the active nucleophile in hydrolysis reactions catalyzed by binuclear hydrolases is a recurrent problem and a matter of intense debate. We report on the phosphate ester hydrolysis by a Fe III Fe II complex of a binucleating ligand. This complex presents activities in the range of those observed for similar biomimetic compounds in the literature. The specific electronic properties of the Fe III Fe II complex allowed us to use 1 H NMR and Mössbauer spectroscopies to investigate the nature of the various species present in the solution in the pH range of 5–10. Both techniques showed that the hydrolysis activity is associated to a μ‐hydroxido Fe III Fe II species. Further 1 H NMR experiments show that binding of anions or the substrate changes this bonding mode suggesting that a terminal hydroxide is the likely nucleophile in these hydrolysis reactions. This view is further supported by the structure determination of the hydrolysis product.