Webb, John Mark (1972) Structural studies of some polynuclear iron proteins. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-02042005-105229
The coordination structure and electronic configuration of iron(III) bound in a polynuclear fashion to a number of proteins have been investigated by a variety of physical methods. These have included the temperature dependence of the magnetic susceptibility, electron spin resonance spectroscopy, electronic absorption spectroscopy at low temperatures, vibrational spectroscopy, X-ray analysis, Mossbauer spectroscopy down to helium temperature, and electron spectroscopy for chemical analysis (ESCA). The proteins investigated included the iron transport protein transferrin, the phosphoglycoprotein phosvitin, the gastric juice glycoprotein gastroferrin, and the two iron storage proteins ferritin and hemosiderin. On the basis of the results obtained by these techniques the structural relationship of the iron to the protein and to other iron atoms present in the polynuclear complex was clarified. Structural models for these relationships were proposed for the proteins listed. The implications of these results for the biological role of iron have been considered.
|Item Type:||Thesis (Dissertation (Ph.D.))|
|Degree Grantor:||California Institute of Technology|
|Division:||Chemistry and Chemical Engineering|
|Thesis Availability:||Public (worldwide access)|
|Defense Date:||30 August 1971|
|Default Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Imported from ETD-db|
|Deposited On:||07 Feb 2005|
|Last Modified:||26 Dec 2012 02:30|
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