ESR spectroscopy identifies inhibitory Cu2+ sites in a DNA-modifying enzyme to reveal determinants of catalytic specificity

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 109; no. 17; pp. E993 - E1000
• Main Authors: Yang, Zhongyu, Kurpiewski, Michael R, Ji, Ming, Townsend, Jacque E, Mehta, Preeti, Jen-Jacobson, Linda, Saxena, Sunil
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 24.04.2012; National Acad Sciences
• Series: PNAS Plus
• Subjects: Biocatalysis; Biological Sciences; calorimetry; catalytic activity; Catalytic Domain; chemistry; Copper; Copper - metabolism; Dimerization; DNA; DNA - metabolism; DNA Modification Methylases; DNA Modification Methylases - chemistry; DNA Modification Methylases - metabolism; Electron Spin Resonance Spectroscopy; Electron Spin Resonance Spectroscopy - methods; histidine; Histidine - metabolism; ions; magnesium; metabolism; methods; molecular dynamics; Molecular Dynamics Simulation; nucleotide sequences; Physical Sciences; PNAS Plus; spectroscopy; titration

The relationship between DNA sequence recognition and catalytic specificity in a DNA-modifying enzyme was explored using paramagnetic Cu2+ ions as probes for ESR spectroscopic and biochemical studies. Electron spin echo envelope modulation spectroscopy establishes that Cu2+ coordinates to histidine...