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Multifield Saturation Magnetization Measurements of Oxidized and Reduced Ribonucleotide Reductase from Escherichia coli
Author(s) -
Atta Mohammed,
Scheer Corinne,
Fries Pascal H.,
Fontecave Marc,
Latour JeanMarc
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199215131
Subject(s) - ribonucleotide reductase , protonation , chemistry , ribonucleotide , magnetization , salt bridge , carboxylate , ferromagnetism , crystallography , stereochemistry , saturation (graph theory) , nucleotide , condensed matter physics , physics , biochemistry , organic chemistry , ion , protein subunit , quantum mechanics , magnetic field , mutant , gene , mathematics , combinatorics
A diiron( II ) center doubly bridged by carboxylate groups (see sketch) is present in reduced ribonucleotide reductase according to magnetization measurements: the strong anti‐ferromagnetic coupling of the oxidized diiron( III ) site consistent with an oxo bridge is no longer observed. Protonation of the oxo bridge during the reduction is postulated. The loss of the resulting aqua bridge then leads to the structural unit shown here.