Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron center
- 21 February 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (4), 1923-1929
- https://doi.org/10.1021/bi00430a074
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 21 references indexed in Scilit:
- Resonance Raman study of the .mu.-oxo-bridged binuclear iron center in oxyhemerythrinJournal of the American Chemical Society, 1984
- Assembly and characterization of an accurate model for the diiron center in hemerythrinJournal of the American Chemical Society, 1984
- Binuclear iron complexes in methemerythrin and azidomethemerythrin at 2.0-.ANG. resolutionJournal of the American Chemical Society, 1984
- Ribonucleotide Reductase—a Radical EnzymeScience, 1983
- Stoichiometric characteristics and Resonance Raman spectra of azidosemimethemerythrinArchives of Biochemistry and Biophysics, 1983
- Raman spectral evidence for a .mu.-oxo bridge in the binuclear iron center of ribonucleotide reductaseBiochemistry, 1982
- Multiple conformations at functional site of hemerythrin: Evidence from resonance Raman spectraProceedings of the National Academy of Sciences, 1981
- The iron center in ribonucleotide reductase from Escherichia coli.Journal of Biological Chemistry, 1980
- A computer-controlled laser Raman spectrophotometer with interactive-graphics data analysisAnalytical Biochemistry, 1979
- The tyrosine free radical in ribonucleotide reductase from Escherichia coli.Journal of Biological Chemistry, 1978