Exploring the Fe(III) Binding Sites of Human Serum Transferrin with EPR at 275 GHz

Overview

Journal J Biol Inorg Chem

Publisher Springer

Specialty Biochemistry

Date 2014 Dec 25

PMID 25537134

Citations 5

Authors

Guinevere Mathies

Peter Gast

N Dennis Chasteen

Ashley N Luck

Anne B Mason

Edgar J J Groenen

Affiliations

Soon will be listed here.

Abstract

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 [Formula: see text] 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.

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