Electron-nuclear double resonance of horseradish peroxidase compound I. Detection of the porphyrin pi-cation radical. Academic Article

abstract

• Electron-nuclear double resonance spectra of horseradish peroxidase Compound I exhibit resonances from 14N and beta-protons, and most probably alpha-protons as well. The measurements prove that the oxyferryl iron of this enzymic intermediate is spin-coupled to a porphyrin radical. Comparison of experimentally obtained average pi-electron spin densities with theoretical predictions for a 4-fold symmetric porphyrin pi-cation radical is supportive of a 2A2u assignment for the radical's electronic state.

authors

• Musser, Siegfried

published proceedings

• J Biol Chem

author list (cited authors)

• Roberts, J. E., Hoffman, B. M., Rutter, R., & Hager, L. P

citation count

• 131

complete list of authors

• Roberts, JE||Hoffman, BM||Rutter, R||Hager, LP

publication date

• March 1981

publisher

• Elsevier BV  Publisher

published in

• Journal of Biological Chemistry  Journal

keywords

• Electron Spin Resonance Spectroscopy
• Free Radicals
• Horseradish Peroxidase
• Isoenzymes
• Macromolecular Substances
• Magnetic Resonance Spectroscopy
• Peroxidases
• Porphyrins
• Protein Binding
• Protein Conformation
• Spin Labels

PubMed Central ID

• 6257699

Digital Object Identifier (DOI)

• 10.1016/s0021-9258(19)69747-4

start page

• 2118

end page

• 2121

volume

• 256

issue

• 5