Study of the Tyrosyl Radical in Epstein-Barr Virus Ribonucleotide Reductase
Author Information
Author(s): Tomter Ane B., Zoppellaro Giorgio, Schmitzberger Florian, Andersen Niels H., Barra Anne-Laure, Engman Henrik, Nordlund Pär, Andersson K. Kristoffer
Primary Institution: Department of Molecular Biosciences, University of Oslo, Oslo, Norway
Hypothesis
The electronic and magnetic properties of the tyrosyl radical in Epstein-Barr virus ribonucleotide reductase R2 can be characterized using various spectroscopic techniques.
Conclusion
The study found that the tyrosyl radical in EBV R2 exhibits unique electromagnetic characteristics, indicating a different kind of tyrosyl radical compared to other studied R2s.
Supporting Evidence
- The tyrosyl radical in EBV R2 shows a g1-value of 2.0080, indicating a positive charge nearby.
- Resonance Raman spectroscopy revealed a C-O stretching frequency at 1508 cm−1 for the tyrosyl radical.
- Comparative studies showed that EBV R2 has a lower affinity for Fe2+ than E. coli R2.
Takeaway
This study looks at a special part of a virus that helps it make DNA, showing how it works differently than similar parts in other organisms.
Methodology
The researchers used EPR, HF-EPR, UV/VIS, and resonance Raman spectroscopy to analyze the tyrosyl radical in EBV R2.
Limitations
The study could not clearly identify a water molecule as a hydrogen bond donor for the tyrosyl radical in EBV R2.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website