Anthraquinone Photonuclease Structure Determines Its Mode of Binding to DNA and the Cleavage Chemistry Observed

摘要

The ability of AQI to footprint netropsin suggests that it reacts, at least in part, from the minor groove. These findings show that simple structural change to the anthrquinone derivative has a profound effects on its binding and chemical properties. We are exploring the detailed reaction mechanisms and applications of these nucleases.