First Evidence of Anchimeric Spin Delocalization in Tryptophan Radical Cation¹

This publication has 9 references indexed in Scilit:

• 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
• Laue diffraction study on the structure of cytochrome c peroxidase compound I
  Structure, 1994
• The Asp-His-iron triad of cytochrome c peroxidase controls the reduction potential electronic structure, and coupling of the tryptophan free radical to the heme
  Biochemistry, 1993
• Crystal Structure of a Complex Between Electron Transfer Partners, Cytochrome c Peroxidase and Cytochrome c
  Science, 1992
• Electron-Tunneling Pathways in Oroteins
  Science, 1992
• Nature of biological electron transfer
  Nature, 1992
• Identification by ENDOR of Trp ¹⁹¹ as the Free-Radical Site in Cytochrome c Peroxidase Compound ES
  Science, 1989
• Gated electron transfer: when are observed rates controlled by conformational interconversion?
  Journal of the American Chemical Society, 1987
• Conformation and interaction of dinucleoside mono- and diphosphates. 2. Influence of the phosphodiester linkage (3'-5', 2'-5', and 5'-5') on the conformation of dinucleoside monophosphate
  Biochemistry, 1970