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Mass spectrometric and calorimetric data reveal that phosphate ion binding to the active site of colicin E9 DNase is delicately regulated by concomitant binding of specific transition metal ions.

Original publication

DOI

10.1039/b415709e

Type

Journal article

Journal

Chem Commun (Camb)

Publication Date

07/03/2005

Pages

1137 - 1139

Keywords

Binding Sites, Calorimetry, Crystallography, X-Ray, Deoxyribonucleases, Escherichia coli Proteins, Mass Spectrometry, Metals, Molecular Structure, Phosphates, Structure-Activity Relationship