Astrid Gräslund
Technical University of Berlin
8 Papers
478 Citations
Astrid Gräslund is an academic researcher from Technical University of Berlin. The author has contributed to research in topics: Ribonucleotide reductase & Radical. The author has an hindex of 6, co-authored 8 publications.
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Papers
The tyrosine free radical in ribonucleotide reductase from Escherichia coli.
TL;DR: Additional isotope substitution experiments now show that the spin density of the radical must be delocalized over the aromatic ring of the tyrosine residue of the enzyme.
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The iron center in ribonucleotide reductase from Escherichia coli.
TL;DR: Determinations by EPR of the amount of free radical suggest the possibility of more than one radical per active protein B2 molecule, and the most likely structure is an antiferromagnetically coupled pair of high spin Fe(III) with a bridging oxo-group.
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A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2'-azido-2'-deoxynucleoside diphosphates.
TL;DR: The present results are consistent with the hypothesis that the appearance and structure of the transient radical mimic stages in the normal reaction pathway of ribonucleotide reductase, postulated to proceed via 3'-hydrogen abstraction and cation radical formation of the substrate nucleotide.
110
Electronic structure of neutral tryptophan radicals in ribonucleotide reductase studied by EPR and ENDOR spectroscopy
Friedhelm Lendzian,Margareta Sahlin,Fraser MacMillan,Robert Bittl,Robert Fiege,Stephan Pötsch,Britt-Marie Sjöberg,Astrid Gräslund,Wolfgang Lubitz,Günter Lassmann +9 more
TL;DR: In this paper, the first detailed hyperfine parameters for protein-linked oxidized neutral tryptophan radicals (Wa• and Wb•) with lifetimes of several minutes at room temperature were derived.
99
Structure of the tyrosyl radical in bacteriophage T4-induced ribonucleotide reductase
TL;DR: When compared to the bacterial ribonucleotide reductase, the T4-induced enzyme shows an overall approximately 10 times higher sensitivity to hydroxyurea, judging from the drug concentrations needed to destroy the radicals and inhibit the activities.
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