PMID:14653724
| Citation |
Bennati, M, Weber, A, Antonic, J, Perlstein, DL, Robblee, J and Stubbe, J (2003) Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl dadicals in the R2 subunit of the E. coli ribonucleotide reductase. J. Am. Chem. Soc. 125:14988-9 |
|---|---|
| Abstract |
Escherichia coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleoside diphosphates (NDPs) to deoxynucleoside diphosphates (dNDPs). This RNR is composed of two homodimeric subunits: R1 and R2. R1 binds the NDPs in the active site, and R2 harbors the essential di-iron tyrosyl radical (Y*) cofactor. In this paper, we used PELDOR, a method that detects weak electron-electron dipolar coupling, to make the first direct measurement of the distance between the two Y*'s on each monomer of R2. In the crystal structure of R2, the Y*'s are reduced to tyrosines, and consequently R2 is inactive. In R2, where the Y*'s assume a well-defined geometry with respect to the protein backbone, the PELDOR method allows measurement of a distance of 33.1 +/- 0.2 A that compares favorably to the distance (32.4 A) between the center of mass of the spin density distribution of each Y* on each R2 monomer from the structure. The experiments provide the first direct experimental evidence for two Y*'s in a single R2 in solution. |
| Links |
PubMed Online version:10.1021/ja0362095 |
| Keywords |
Computer Simulation; Electron Spin Resonance Spectroscopy/methods; Escherichia coli/enzymology; Free Radicals/chemistry; Ribonucleotide Reductases/chemistry; Tyrosine/chemistry |
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