A1 Journal article – refereed
Cd2+-induced aggregation of Escherichia coli pyrophosphatase




List of Authors: Zimenkov YV, Salminen A, Efimova IS, Lahti R, Baykov AA
Publisher: BLACKWELL PUBLISHING LTD
Publication year: 2004
Journal: European Journal of Biochemistry
Journal name in source: EUROPEAN JOURNAL OF BIOCHEMISTRY
Journal acronym: EUR J BIOCHEM
Volume number: 271
Issue number: 14
ISSN: 0014-2956

Abstract
We report here that Escherichia coli pyrophosphatase aggregates in the presence of millimolar Cd2+. This highly cooperative process was specific to both the metal ion and the protein and could be reversed fully by decreasing the Cd2+ concentration. Aggregation was enhanced by Mg2+, the natural cofactor of pyrophosphatase, and Mn2+. Mutations at the intersubunit metal-binding site had no effect, whereas mutation at Glu139, which is part of the peripheral metal-binding site found in pyrophosphatase crystals near the contact region between two enzyme molecules, suppressed aggregation. These findings indicate that aggregation is affected by Cd2+ binding to the peripheral metal-binding site, probably by strengthening intermolecular Trp149-Trp149' stacking interactions.

Last updated on 2019-29-01 at 21:42