title: Mössbauer studies on iron(II)-substituted yeast metallothionein.
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.
authors.affiliation: Institut für Physik, Medizinische Universität Lübeck, Germany.
authors.forename: X Q
authors.initials: XQ
authors.lastname: Ding
authors.forename: E
authors.initials: E
authors.lastname: Bill
authors.forename: A X
authors.initials: AX
authors.lastname: Trautwein
authors.forename: H J
authors.initials: HJ
authors.lastname: Hartmann
authors.forename: U
authors.initials: U
authors.lastname: Weser
mesh_terms: D001059:Apoproteins / Q000737:chemistry; D005296:Ferrous Compounds / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008280:Magnetics; D008668:Metallothionein / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D015204:Spectroscopy, Mossbauer; D017186:Titrimetry
chemical_list: D001059:Apoproteins; D005296:Ferrous Compounds; D008668:Metallothionein; D007501:Iron