Electronic Structure of Neutral Tryptophan Radicals in Ribonucleotide Reductase Studied by EPR and ENDOR Spectroscopy

This publication has 32 references indexed in Scilit:

• Enzymic and Chemical Reduction of the Iron Center of the Escherichia coli Ribonucleotide Reductase Protein R2
  European Journal of Biochemistry, 1995
• Compound ES of Cytochrome c Peroxidase Contains a Trp .pi.-Cation Radical: Characterization by Continuous Wave and Pulsed Q-Band External Nuclear Double Resonance Spectroscopy
  Journal of the American Chemical Society, 1995
• Structure of ribonucleotide reductase protein R1
  Nature, 1994
• 3-mm High-field EPR on semiquinone radical anions Q.cntdot.- related to photosynthesis and on the primary donor P.cntdot.+ and acceptor QA.cntdot.- in reaction centers of Rhodobacter sphaeroides R-26
  The Journal of Physical Chemistry, 1993
• Structure and Function of the Escherichia coli Ribonucleotide Reductase Protein R2
  Journal of Molecular Biology, 1993
• EPR stopped-flow studies of the reaction of the tyrosyl radical of protein r2 from ribonucleotide reductase with hydroxyurea
  Biochemical and Biophysical Research Communications, 1992
• Single-photon and multiphoton dissociation of molybdenum hexacarbonyl at 248 nm
  The Journal of Physical Chemistry, 1991
• ENDOR analysis of H-addition radicals and their conversion in irradiated crystals of tryptamine hydrochloride
  The Journal of Chemical Physics, 1983
• An ESR Study of Irradiated L-Tryptophan·HCl Single Crystals at 295 K
  Radiation Research, 1978
• Hindered Internal Rotation and ESR Spectroscopy
  The Journal of Chemical Physics, 1962