High Field EPR Studies of Mouse Ribonucleotide Reductase Indicate Hydrogen Bonding of the Tyrosyl Radical
Open Access
- 1 September 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (39) , 23615-23618
- https://doi.org/10.1074/jbc.271.39.23615
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Ribonucleotide reductases: radical enzymes with suicidal tendenciesChemistry & Biology, 1995
- Diiron–Oxygen ProteinsPublished by Elsevier ,1995
- Structure of Ribonucleotide Reductase from Escherichia coliPublished by Springer Nature ,1995
- Structure of ribonucleotide reductase protein R1Nature, 1994
- Structure and Function of the Escherichia coli Ribonucleotide Reductase Protein R2Journal of Molecular Biology, 1993
- From RNA to DNA, Why So Many Ribonucleotide Reductases?Science, 1993
- Using saturation-recovery EPR to measure exchange couplings in proteins: application to ribonucleotide reductaseJournal of the American Chemical Society, 1992
- Three-dimensional structure of the free radical protein of ribonucleotide reductaseNature, 1990
- Tyrosine radicalsTrends in Biochemical Sciences, 1988
- Magnetic interaction between the tyrosyl free radical and the antiferromagnetically coupled iron center in ribonucleotide reductaseBiochemistry, 1987