Mössbauer studies on iron(II)‐substituted yeast metallothionein

Xiao‐Qi ‐Q DING, Eckhard BILL, Alfred Xaver TRAUTWEIN*, Hans‐Jürgen ‐J HARTMANN, Ulrich WESER

*Corresponding author for this work
8 Citations (Scopus)


Iron(II)‐substituted yeast metallothionein has been studied with Mössbauer 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.

Original languageEnglish
JournalEuropean Journal of Biochemistry
Issue number3
Pages (from-to)841-845
Number of pages5
Publication statusPublished - 01.08.1994


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