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J. Biol. Chem., Vol. 275, Issue 21, 15828-15831, May 26, 2000
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From the Department of Chemistry, Indiana University, Bloomington,
Indiana 47405
The repair of phosphodiester bonds in nicked DNA
is catalyzed by DNA ligases. Ligation is coupled to cleavage of a
phosphoanhydride bond in a nucleotide cofactor resulting in a
thermodynamically favorable process. A free energy value for
phosphodiester bond formation was calculated using the reversibility of
the T4 DNA ligase reaction. The relative number of DNA nicks to
phosphodiester bonds in a circular plasmid DNA, formed during this
reaction at fixed concentrations of ATP to AMP and
PPi, was quantified. At 25 °C, pH 7, the
equilibrium constant (Keq) for the ligation
reaction is 3.89 × 104 M. This value
corresponds to a standard free energy (
Determination of the Free-Energy Change for Repair of a DNA
Phosphodiester Bond*
,
G°') of 
6.3 kcal
mol
1. By subtracting the known energy contribution due to
hydrolysis of ATP to AMP and PPi, G°' for the
hydrolysis of a DNA phosphodiester bond is 5.3 kcal
mol1.
*
This research was supported by Grant GM 56095 from the
National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Biochemistry, University of Wisconsin,
Madison, WI 53706.
§
Present address: Nuffield Dept. of Clinical Biochemistry,
University of Oxford, Inst. of Molecular Medicine, John Radcliffe Hospital, Oxford OX3 D9S, United Kingdom.
¶
To whom correspondence should be addressed: Dept. of
Chemistry, Indiana University, 800 E. Kirkwood Ave., Bloomington, IN 47405. Tel.: 812-855-1520; Fax: 812-855-8300; E-mail:
richardj@indiana.edu.
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