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REVIEW: Mechanism of Recognition and Repair of Damaged DNA by Human 8-Oxoguanine DNA Glycosylase hOGG1

N. A. Kuznetsov, V. V. Koval, and O. S. Fedorova*

Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Akademika Lavrent’eva 8, 630090 Novosibirsk, Russia; fax: (383) 363-5153; E-mail: fedorova@niboch.nsc.ru

* To whom correspondence should be addressed.

Received July 7, 2010; Revision received August 17, 2010
Recent data on structural and biochemical features of human 8-oxoguanine DNA glycosylase (hOGG1) has enabled detailed evaluation of the mechanism by which the damaged DNA bases are recognized and eliminated from the chain. Pre-steady-state kinetic studies with recording of conformational transitions of the enzyme and DNA substrate significantly contribute to understanding of this mechanism. In this review we particularly focus on the interrelationship between the conformational changes of interacting molecules and kinetics of their interaction and on the nature of each elementary step during the enzymatic process. Exhaustive analysis of these data and detailed mechanism of hOGG1-catalyzed reaction are proposed.
KEY WORDS: conformational dynamics, pre-steady-state kinetics, human 8-oxoguanine DNA glycosylase, hOGG1

DOI: 10.1134/S0006297911010123