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Biochemical and Biophysical Research Communications|September 15, 1993
19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and methane monooxygenaseS Hamman, M Atta, A Ehrenberg, et al.Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine|June 1, 2000
Iron and citric acid: a fuzzy chemistry of ubiquitous biological relevanceJ L Pierre, I Gautier-LuneauBiometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine|August 18, 2001
Old iron, young copper: from Mars to VenusR R Crichton, J L PierreBiochimica Et Biophysica Acta|March 15, 1995
NMR studies of binding of 5-FdUDP and dCDP to ribonucleoside-diphosphate reductase from Escherichia coliB Roy, J L Decout, C Béguin, et al.The Biochemical Journal|March 15, 1993
Escherichia coli and herpes-simplex-virus ribonucleotide reductase R2 subunit. Compared reactivities of the redox centresM Atta, N Lamarche, J P Battioni, et al.Biochemistry|July 2, 1996
Inactivation of Escherichia coli ribonucleotide reductase by 2'-deoxy-2'-mercaptouridine 5'-diphosphate. Electron paramagnetic resonance evidence for a transient protein perthiyl radicalJ Covès, L Le Hir de Fallois, L Le Pape, et al.Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|April 9, 2018
Spectroscopic investigations of a semi-synthetic [FeFe] hydrogenase with propane di-selenol as bridging ligand in the binuclear subsite: comparison to the wild type and propane di-thiol variantsC Sommer, S Rumpel, S Roy, et al.The Journal of Biological Chemistry|December 15, 1992
Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coliR Eliasson, E Pontis, M Fontecave, et al.Biochemical and Biophysical Research Communications|December 15, 1993
Flavodoxin is required for the activation of the anaerobic ribonucleotide reductaseV Bianchi, R Eliasson, M Fontecave, et al.The Biochemical Journal|November 15, 1996
Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacityN Lamarche, G Matton, B Massie, et al.Pageof 12