PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase.
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.
Max Planck Institute for Bioinorganic Chemistry, D-45470 Mülheim an der Ruhr, Germany.
Daniele
D
Biglino
Peter P
PP
Schmidt
Edward J
EJ
Reijerse
Wolfgang
W
Lubitz
D000818:Animals; D019281:Dimerization; D004578:Electron Spin Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods*; D004926:Escherichia coli / Q000201:enzymology; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D012264:Ribonucleotide Reductases / Q000737:chemistry*; D014443:Tyrosine / Q000737:chemistry*
D014443:Tyrosine; D012264:Ribonucleotide Reductases; C108427:ribonucleotide reductase R2 subunit