hf-epr, raman, uvvis light spectroscopic, and dft studies of the ribonucleotide reductase r2 tyrosyl radical from epstein-barr virushf-epr,拉曼、依照此光光谱和dft的研究从巴尔病毒核苷酸还原酶r2酪氨酰激进.pdfVIP

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hf-epr, raman, uvvis light spectroscopic, and dft studies of the ribonucleotide reductase r2 tyrosyl radical from epstein-barr virushf-epr,拉曼、依照此光光谱和dft的研究从巴尔病毒核苷酸还原酶r2酪氨酰激进.pdf

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hf-epr, raman, uvvis light spectroscopic, and dft studies of the ribonucleotide reductase r2 tyrosyl radical from epstein-barr virushf-epr,拉曼、依照此光光谱和dft的研究从巴尔病毒核苷酸还原酶r2酪氨酰激进

HF-EPR, Raman, UV/VIS Light Spectroscopic, and DFT Studies of the Ribonucleotide Reductase R2 Tyrosyl Radical from Epstein-Barr Virus 1 1 2¤ 1 3 Ane B. Tomter , Giorgio Zoppellaro , Florian Schmitzberger , Niels H. Andersen , Anne-Laure Barra , 2 ¨ 2 1 Henrik Engman , Par Nordlund , K. Kristoffer Andersson * 1 Department of Molecular Biosciences, University of Oslo, Oslo, Norway, 2 Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden, ´ 3 Laboratoire National des Champs Magnetiques Intenses, LNCMI-G, UPR 3228, CNRS, Grenoble, France Abstract Epstein-Barr virus (EBV) belongs to the gamma subfamily of herpes viruses, among the most common pathogenic viruses in humans worldwide. The viral ribonucleotide reductase small subunit (RNR R2) is involved in the biosynthesis of nucleotides, the DNA precursors necessary for viral replication, and is an important drug target for EBV. RNR R2 generates a stable tyrosyl radical required for enzymatic turnover. Here, the electronic and magnetic properties of the tyrosyl radical in EBV R2 have been determined by X-band and high-field/high-frequency electron paramagnetic resonance (EPR) spectroscopy recorded at cryogenic temperatures. The radical exhibits an unusually low g1-tensor component at 2.0080, indicative of a positive charge in the vicinity of the radical. Consistent with these EPR results a relatively high C-O stretching frequency associated with the phenoxyl radical (at 1508 cm 21) is observed with resonance Raman spectroscopy. In contrast to mouse R2,