Exploring the Fe(III) binding sites of human serum transferrin with EPR at 275 GHz

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• 作者：Guinevere Mathies (1) (2)
  Peter Gast (1)
  N. Dennis Chasteen (3)
  Ashley N. Luck (4)
  Anne B. Mason (4)
  Edgar J. J. Groenen (1)
  
  1. Department of Physics ; Huygens-Kamerlingh Onnes Laboratory ; Leiden University ; Leiden ; The Netherlands
  2. Department of Chemistry ; Francis Bitter Magnet Laboratory ; Massachusetts Institute of Technology ; Cambridge ; MA ; 02139 ; USA
  3. Department of Chemistry ; Parsons Hall ; University of New Hampshire ; Durham ; NH ; 03824 ; USA
  4. Department of Biochemistry ; University of Vermont College of Medicine ; Burlington ; VT ; 05405 ; USA
  
• 关键词：High ; frequency EPR ; High ; spin $$\text{Fe}^{3+}$$ Fe 3 + ; Human serum transferrin ; Zero ; field splitting
• 刊名：Journal of Biological Inorganic Chemistry
• 出版年：2015
• 出版时间：April 2015
• 年：2015
• 卷：20
• 期：3
• 页码：487-496
• 全文大小：1,439 KB
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• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Microbiology
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1432-1327

文摘

We report 275 GHz EPR spectra of human serum transferrin. At this high microwave frequency the zero-field splitting between the magnetic sublevels of the high-spin \(\text{Fe}^{3+}\) sites can be accurately determined. We find the zero-field splitting to be a sensitive probe of the structure of the transferrin iron-binding sites. Signals arising from iron bound to the transferrin N-lobe can clearly be distinguished from signals from iron bound to the C-lobe. Moreover, our spectra show that the structure of the iron site in the N-lobe is influenced by the presence and conformation of the C-lobe. The spectra of a series of N-lobe mutants altering the second-shell interaction of Arg124 with the synergistic anion carbonate reflect conformational changes induced at the iron site.