TY - JOUR
T1 - Mechanism of o-phenanthroline mediated inhibition of E. coli DNA polymerase I
T2 - Formation of template-primer-metal-phenanthroline complexes with resultant loss of catalytic activity
AU - Abraham, Kakkudiyil I.
AU - Modak, Mukund J.
N1 - Funding Information:
ACKNOWLEDGEMENTS: This research was supported by a grant from NIH and by a research career development award# i K04 CA-545 to MJM.
PY - 1983/9/15
Y1 - 1983/9/15
N2 - 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.
AB - 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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U2 - 10.1016/S0006-291X(83)80182-X
DO - 10.1016/S0006-291X(83)80182-X
M3 - Article
C2 - 6354184
AN - SCOPUS:0020601875
VL - 115
SP - 567
EP - 576
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -