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pubmed-article:8805591pubmed:abstractTextRibonucleotide reductases (RNRs) catalyze the formation of the deoxyribonucleotides that are essential for DNA synthesis. The R2 subunit of Escherichia coli RNR is a homodimer containing one dinuclear iron centre per monomer. A tyrosyl radical is essential for catalysis, and is formed via a reaction in which the reduced, diferrous form of the iron centre activates dioxygen. To help understand the mechanism of oxygen activation, we examined the structure of the diferrous form of R2.lld:pubmed
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pubmed-article:8805591pubmed:articleTitleCrystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site.lld:pubmed
pubmed-article:8805591pubmed:affiliationDepartment of Molecular Biology University of Stockholm S-106 91 Stockholm Sweden.lld:pubmed
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