Mössbauer investigations of high-spin ferrous heme proteins

"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."

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Physics

Year dc:date

2012

Author dc:creator

• Champion, Paul Morris

Contributors dc:contributor

• Debrunner, Peter G.

• Mössbauer investigations
• heme proteins
• Mössbauer spectroscopy
• cytochrome P-450
• ch1oroperoxidase
• horseradish peroxidase
• hemoglobin

Statement dc:rights

• ©1975 Champion

Language dc:language

en

Identifier

2299522

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/30735