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Cover Picture: In‐Cell Characterization of the Stable Tyrosyl Radical in E. coli Ribonucleotide Reductase Using Advanced EPR Spectroscopy (Angew. Chem. Int. Ed. 35/2021)
Author(s) -
Meichsner Shari L.,
Kutin Yury,
Kasanmascheff Müge
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202109131
Subject(s) - ribonucleotide reductase , electron paramagnetic resonance , chemistry , ribonucleotide , enzyme , dna , spectroscopy , bioinorganic chemistry , stereochemistry , biochemistry , biophysics , nucleotide , biology , nuclear magnetic resonance , physics , protein subunit , gene , quantum mechanics
The structure and regulation of the tyrosyl radical in ribonucleotide reductase in whole E. coli cells was investigated by using advanced EPR spectroscopy. This radical starts the biosynthesis of DNA building blocks, and is thus involved in essential processes in life. The observations reported by Müge Kasanmascheff et al. in their Research Article on page 19155 were surprising and exciting because the findings indicated a distinct radical distribution within the cells, pointing to a complex regulation mechanism of this fundamental enzyme in its native environment.