Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism
- 1 January 1997
- book chapter
- Published by Springer Nature
- p. 139-173
- https://doi.org/10.1007/3-540-62870-3_5
Abstract
No abstract availableKeywords
This publication has 120 references indexed in Scilit:
- The Ten-stranded β/α Barrel in Ribonucleotide Reductase Protein R1Journal of Molecular Biology, 1996
- Iron ligand mutants in protein R2 of Escherichia coli ribonucleotide reductaseJBIC Journal of Biological Inorganic Chemistry, 1996
- Sequence Analysis of the Genome of the Unicellular Cyanobacterium Synechocystis sp. Strain PCC6803. II. Sequence Determination of the Entire Genome and Assignment of Potential Protein-coding RegionsDNA Research, 1996
- TO BE THERE WHEN THE PICTURE IS PAINTEDAnnual Review of Biochemistry, 1995
- Electron Paramagnetic Resonance Evidence for a Cysteine-Based Radical in Pyruvate Formate-lyase Inactivated with MercaptopyruvateBiochemistry, 1995
- Structure of ribonucleotide reductase protein R1Nature, 1994
- Structure and Function of the Escherichia coli Ribonucleotide Reductase Protein R2Journal of Molecular Biology, 1993
- A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coliBiochemical and Biophysical Research Communications, 1991
- Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron centerBiochemistry, 1989
- Characterization of the Active Site of Ribonucleotide Reductase of Escherichia coli, Bacteriophage T4 and Mammalian Cells by Inhibition Studies with Hydroxyurea AnaloguesEuropean Journal of Biochemistry, 1982