Structure of the Nucleotide Radical Formed during Reaction of CDP/TTP with the E441Q-α2β2 of E. coli Ribonucleotide Reductase

Structure of the Nucleotide Radical Formed during Reaction of CDP/TTP with the E441Q-α2β2 of E. coli Ribonucleotide Reductase

The Escherichia coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleoside diphosphates to deoxynucleotides and requires a diferric-tyrosyl radical cofactor for catalysis. RNR is composed of a 1:1 complex of two homodimeric subunits: α and β. Incubation of the E441Q-α mutant RNR with...

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Bibliographic Details
Main Authors: Zipse, Hendrik (Author), Artin, Erin (Contributor), Wnuk, Stanislaw (Author), Lohman, Gregory J. S. (Contributor), Martino, Debora (Contributor), Griffin, Robert Guy (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Chemistry (Contributor), Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology) (Contributor)
Format: Article
Language:English
Published: American Chemical Society (ACS), 2012-10-18T17:11:49Z.
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