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J Am Chem Soc. 2012 Dec 5;134(48):19839-50. doi: 10.1021/ja309082k. Epub 2012 Nov 26.

Gas-phase studies of substrates for the DNA mismatch repair enzyme MutY.

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1
Department of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, New Brunswick, New Jersey 08901, United States.

Abstract

The gas-phase thermochemical properties (tautomeric energies, acidity, and proton affinity) have been measured and calculated for adenine and six adenine analogues that were designed to test features of the catalytic mechanism used by the adenine glycosylase MutY. The gas-phase intrinsic properties are correlated to possible excision mechanisms and MutY excision rates to gain insight into the MutY mechanism. The data support a mechanism involving protonation at N7 and hydrogen bonding to N3 of adenine. We also explored the acid-catalyzed (non-enzymatic) depurination of these substrates, which appears to follow a different mechanism than that employed by MutY, which we elucidate using calculations.

PMID:
23106240
PMCID:
PMC4204490
DOI:
10.1021/ja309082k
[Indexed for MEDLINE]
Free PMC Article
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