Mossbauer studies on iron(II)-substituted yeast metallothionein
1994
Ding, X.Q. | Bill, E. | Trautwein, A.X. | Hartmann, H.J. | Weser, U.
Iron(II)-substituted yeast metallothionein has been studied with Mossbauer spectroscopy. The iron in the protein is in the high-spin ferrous state. A maximum metal content of four iron(II)/ molecule has been determined, with the four metal ions forming a diamagnetic cluster due to the antiferromagnetic exchange interaction between Fe2+ via bridging thiolates. In the case where the iron titration gives a value of less than four iron(II)/apoprotein, the metal ions are magnetically non-interacting, with each individual iron(II) behaving like iron(II) in reduced rubredoxin.
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