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Allosteric Regulation of Artificial Phosphoesterase Activity by Metal Ions
Author(s) -
Fritsky Igor O.,
Ott Reina,
Krämer Roland
Publication year - 2000
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20000915)39:18<3255::aid-anie3255>3.0.co;2-7
Subject(s) - allosteric regulation , chemistry , computer science , biochemistry , enzyme
Allosteric control of the activity of a low molecular weight catalyst by metal ions is demonstrated for the first time. In the trinuclear complex 1 two Cu 2+ ions cooperate in the cleavage of the phosphodiester HPNP, while a third metal ion (M) is not directly involved in catalysis but is expected to create more or less reactive conformations of the catalyst. Relative reactivities for M=Pd II , Ni II , and Cu II are 1:3:10.