Simulation of the EMR Spectra of High-Spin Iron in Proteins

  • Betty J. Gaffney
  • Harris J. Silverstone
Part of the Biological Magnetic Resonance book series (BIMR, volume 13)


Very detailed information about the energy levels and orientations of d orbitals in heme proteins has been obtained by combining EMR studies of paramagnetic samples with other structural information from X-ray crystallography and optical studies. As a result, the chemistry of heme enzymes can be discussed in detail. While the aim of this chapter is to review progress in bringing the chemistry of mononuclear iron centers in nonheme proteins to a similar level of knowledge, our understanding of line shape analysis for high-spin iron is dominated by the vast literature on heme samples. We begin this introduction with some of the history of EMR spectroscopy of methemoglobin and metmyoglobin.


Heme Protein Freeze Solution Resonance Field Phenylalanine Hydroxylase Powder Spectrum 
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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Betty J. Gaffney
    • 1
  • Harris J. Silverstone
    • 1
  1. 1.Department of ChemistryThe Johns Hopkins UniversityBaltimoreUSA

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