PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase

Phys Chem Chem Phys. 2006 Jan 7;8(1):58-62. doi: 10.1039/b513950c. Epub 2005 Nov 21.

Abstract

Pulse electron-electron double resonance (PELDOR) has been employed to measure the distance between the putative tyrosyl radicals in the two halves of the R2 subunit from mouse ribonucleotide reductase. The results provide experimental evidence that the active, tyrosyl radical containing mouse R2 subunit forms a homodimeric form in solution. The distance between the two tyrosyl radicals present in the dimer was determined to be 3.25 +/- 0.05 nm.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Dimerization
  • Electron Spin Resonance Spectroscopy / instrumentation
  • Electron Spin Resonance Spectroscopy / methods*
  • Escherichia coli / enzymology
  • Mice
  • Models, Molecular
  • Protein Conformation
  • Ribonucleotide Reductases / chemistry*
  • Tyrosine / chemistry*

Substances

  • Tyrosine
  • Ribonucleotide Reductases
  • ribonucleotide reductase R2 subunit