Metal induced selectivity in phosphate ion binding in E9 DNase

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.

Saved in:
Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2005-03 (9), p.1137-1139
Main Authors: van den Bremer, Ewald T J, Keeble, Anthony H, Kleanthous, Colin, Heck, Albert J R
Format: Article
Language:English
Subjects:
Binding Sites
Calorimetry
Crystallography, X-Ray
Deoxyribonucleases - chemistry
Deoxyribonucleases - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Mass Spectrometry
Metals - chemistry
Molecular Structure
Phosphates - chemistry
Structure-Activity Relationship
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/b415709e