Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site
- 1 September 1996
- Vol. 4 (9) , 1053-1064
- https://doi.org/10.1016/s0969-2126(96)00112-8
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Gating Effects of Component B on Oxygen Activation by the Methane Monooxygenase Hydroxylase ComponentJournal of Biological Chemistry, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Structure and Function of the Escherichia coli Ribonucleotide Reductase Protein R2Journal of Molecular Biology, 1993
- The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductaseFEBS Letters, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Mechanism of Assembly of the Tyrosyl Radical-Dinuclear Iron Cluster Cofactor of Ribonucleotide ReductaseScience, 1991
- A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coliBiochemical and Biophysical Research Communications, 1991
- Activation of the iron-containing B2 protein of ribonucleotide reductase by hydrogen peroxideBiochemical and Biophysical Research Communications, 1990
- New crystal forms of the small subunit of ribonucleotide reductase from Escherichia coliFEBS Letters, 1989
- Reduced forms of the iron-containing small subunit of ribonucleotide reductase from Escherichia coliBiochemistry, 1989