Abstract
Inhibition of E. coli DNA polymerase I activity by 1,10 phenanthroline in the absence of reducing agents requires a high concentration of inhibitor (1–10 mM) depending upon the template primer used to direct the synthesis. We find that o-phenanthroline, unlike its non-chelating analogue, forms a divalent cation mediated complex with template-primers. Enzyme bound to such complexes is unable to catalyse either polymerization or nuclease functions.
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More From: Biochemical and Biophysical Research Communications
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