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Characterization of the free radical in a plant ribonucleotide reductase
Author(s) -
Harder Jens,
Follmann Hartmut
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80214-4
Subject(s) - ribonucleotide reductase , chemistry , electron paramagnetic resonance , ribonucleotide , biochemistry , deoxyribonucleotide , enzyme , reductase , tyrosine , biosynthesis , protein subunit , stereochemistry , nucleotide , gene , physics , nuclear magnetic resonance
Ribonucleotide reductase of the green alga, Scenedesmus obliquus , contains an organic free radical in its catalytic subunit U2 which is quenched by hydroxyurea and regenerated upon aerobic incubation in the presence of Fe 2+ . The low‐temperature EPR spectrum exhibits a doublet centered at g = 2.0046. This EPR signal is indistinguishable from that of the tyrosine radical in mouse cell ribonucleotide reductase, indicating that the eukaryotes possess one common enzyme apparatus for deoxyribonucleotide biosynthesis.