Mössbauer studies on iron(II)-substituted yeast metallothionein.
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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Institut für Physik, Medizinische Universität Lübeck, Germany.
Bill
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Trautwein
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Hartmann
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Weser
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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
D001059:Apoproteins; D005296:Ferrous Compounds; D008668:Metallothionein; D007501:Iron