University of Illinois Urbana-Champaign

Mössbauer investigations of high-spin ferrous heme proteins

Champion, Paul Morris

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https://hdl.handle.net/2142/30735

Description

Title
Mössbauer investigations of high-spin ferrous heme proteins
Author(s)
Champion, Paul Morris
Issue Date
1975
Doctoral Committee Chair(s)
Debrunner, Peter G.
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
  • Mössbauer investigations
  • heme proteins
  • Mössbauer spectroscopy
  • cytochrome P-450
  • ch1oroperoxidase
  • horseradish peroxidase
  • hemoglobin
Language
en
Abstract
"Mössbauer spectroscopy of heme proteins containing iron in the high-spin ferrous state is discussed. Paramagnetic hyperfine interactions, induced by strong applied magnetic fields, result in Mössbauer spectra that contain a wealth of information about the symmetry of the active site iron atomo Quantitative evaluation of the data relies on a spin Hamiltonian formalism that appears to work quite we110 Model calculations utilizing low-symmetry (tric1inic) crystal fields have also been developed and applied to the data. In addition, comparative studies yield information pertaining to the axial ligands of cytochrome P-450, ch1oroperoxidase, horseradish peroxidase and hemoglobin. A technique that allows the determination of zero-field splitting parameters in high-spin ferrous compounds is also described. This method does not depend on sample concentration, and ""non-iron"" spin impurities do not affect the resu1tso Application to ferrous f1uosilicate yields a value of D 15 K that is compatible with magnetic susceptibility investigations."
Type of Resource
text
Permalink
http://hdl.handle.net/2142/30735
Copyright and License Information
©1975 Champion

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