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Mössbauer studies on iron(II)-substituted yeast metallothionein.

Authors
  • Ding, X Q
  • Bill, E
  • Trautwein, A X
  • Hartmann, H J
  • Weser, U
Type
Published Article
Journal
European journal of biochemistry / FEBS
Publication Date
Aug 01, 1994
Volume
223
Issue
3
Pages
841–845
Identifiers
PMID: 8055961
Source
Medline
License
Unknown

Abstract

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 noninteracting, with each individual iron(II) behaving like iron(II) in reduced rubredoxin.

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