Mössbauer studies on yeast metallothionein

X. Q. Ding*, E. Bill, A. X. Trautwein, H. J. Hartmann, U. Weser

*Corresponding author for this work


Iron-substituted yeast metallothionein, Fe(II)-yeast-MT, has been studied by Mössbauer spectroscopy. The iron in the protein is in the high-spin ferrous state. As maximum metal content, 4 Fe(II)/molecule has been determined, with the 4 metal ions forming a diamagnetic cluster due to the antiferromagnetic exchange interaction between the Fe(II) ions via bridging thiolates. In case the iron titration is less than 4 Fe(II)/apoprotein, the ions are magnetically noninteracting, with each individual Fe(II) behaving similar to Fe(II) in reduced rubredoxin.

Original languageEnglish
JournalHyperfine Interactions
Issue number1
Pages (from-to)791-795
Number of pages5
Publication statusPublished - 01.12.1994


Dive into the research topics of 'Mössbauer studies on yeast metallothionein'. Together they form a unique fingerprint.

Cite this