Article
Dioxygen is the source of the mu-oxo bridge in iron ribonucleotide reductase.
The Journal of biological chemistry - 25 Feb 1994
Ling J, Sahlin M, Sjöberg B M, Loehr T M, Sanders-Loehr J
Abstract excerpt
The formation of the iron-radical cofactor in the R2 subunit of ribonucleotide reductase has been monitored by resonance Raman spectroscopy. The differrous cluster in reduced R2 functions as a tyrosine oxidase; it uses O2 to oxidize Tyr-122 to a stable radical and results in an oxo-bridged diferric cluster. The Phe-122 mutant produces an identical dinuclear iron center and provides a simplified model for O2...
Topics
- Catechols
- Iron
- Mutation
- Oxygen
- Ribonucleotide Reductases
- Spectrum Analysis, Raman