A nuclear magnetic resonance and stopped flow kinetic study of an electron transfer protein, cytochrome c peroxidase
Erman, James E.
M.S. (Master of Science)
Department of Chemistry
Cytochrome c; Proton magnetic resonance spectroscopy
The proton magnetic resonance spectrum of the electron transfer protein cytochrome c peroxidase and its cyano, azido, and fluoro complexes have been measured at 60, 100, and 360 MHz. Also Complex I was measured at 360 MHz. Resonances that are due to the heme substituents which are shifted downfield from the normal diamagnetic region of the NMR spectrum are presented and compared with other ferric heme proteins. In conjunction with the NMR study, a comparison kinetic study of ligand binding of cytochrome c peroxidase and of the cytochrome c peroxidase/cytochrome c complex was made using hydrogen peroxide and fluoride. In the stopped flow study it was found that the cytochrome c peroxidase/cytochrome c complex reacted as fast as cytochrome c peroxidase itself indicating that the complex does not hinder ligand binding of the cytochrome c peroxidase. The resulting k[sub a]'s and k[sub d]'s are compared and discussed with other reported values.
Hoth, Lawrence R., "A NMR and stopped flow kinetic study of an electron transfer protein, cytochrome c peroxidase" (1982). Graduate Research Theses & Dissertations. 438.
v, 51 pages
Northern Illinois University
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Includes bibliographical references.||Includes illustrations.