Activation of the anaerobic ribonucleotide reductase from Escherichia coli by S-adenosylmethionine. Journal of Biological Chemistry 267(35): 25548-25552, 1992
Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein. Journal of Bacteriology 175(6): 1590-1595, 1993
Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli. Journal of Biological Chemistry 267(35): 25541-25547, 1992
Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 92(19): 8759-8762, 1995
Iron-sulfur interconversions in the anaerobic ribonucleotide reductase from Escherichia coli. Journal of Biological Inorganic Chemistry: Jbic: a Publication of the Society of Biological Inorganic Chemistry 4(5): 614-620, 1999
The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681. Journal of Biological Chemistry 271(12): 6827-6831, 1996
Allosteric control of the substrate specificity of the anaerobic ribonucleotide reductase from Escherichia coli. Journal of Biological Chemistry 269(42): 26052-26057, 1994
The anaerobic ribonucleotide reductase from Escherichia coli: The small protein is an activating enzyme containing a (4Fe-4S)2+ center. Journal of Biological Chemistry 274(44): 31291-31296, 1999
The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron sulfur center. Journal of Biological Chemistry 271(16): 9410-9416, 1996
The anaerobic ribonucleotide reductase from Escherichia coli. The small protein is an activating enzyme containing a [4fe-4s](2+) center. Journal of Biological Chemistry 274(44): 31291-31296, 1999
The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy. Biochemical and Biophysical Research Communications 214(1): 28-35, 1995
An iron-sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli. Journal of Biological Chemistry 268(4): 2296-2299, 1993
Interactions of 2'-modified azido- and haloanalogs of deoxycytidine 5'-triphosphate with the anaerobic ribonucleotide reductase of Escherichia coli. Journal of Biological Chemistry 269(42): 26116-26120, 1994
Mass spectrometric determination of the radical scission site in the anaerobic ribonucleotide reductase of Escherichia coli. Biochemical and Biophysical Research Communications 206(2): 731-735, 1995
The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines. Journal of Biological Chemistry 275(21): 15669-15675, 2000