Cd(2+)-induced aggregation of Escherichia coli pyrophosphatase

European Journal of Biochemistry
Yury V ZimenkovA A Baykov

Abstract

We report here that Escherichia coli pyrophosphatase aggregates in the presence of millimolar Cd(2+). This highly cooperative process was specific to both the metal ion and the protein and could be reversed fully by decreasing the Cd(2+) concentration. Aggregation was enhanced by Mg(2+), the natural cofactor of pyrophosphatase, and Mn(2+). 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 Cd(2+) binding to the peripheral metal-binding site, probably by strengthening intermolecular Trp149-Trp149' stacking interactions.

References

Jul 1, 1974·Archives of Biochemistry and Biophysics·R E MillerE R Stadtman
Jul 28, 1999·Applied Microbiology and Biotechnology·D H Nies
Aug 17, 1999·Progress in Molecular and Subcellular Biology·A A BaykovR Lahti
May 1, 1996·Acta Crystallographica. Section D, Biological Crystallography·J KankareA Goldman

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Citations

Sep 15, 2009·Aquatic Toxicology·Meng-Jiao Wang, Wen-Xiong Wang
May 21, 2009·Environmental Science & Technology·John H PriesterPatricia A Holden
Oct 26, 2021·The Science of the Total Environment·Zhaodong LiuJun Luo

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