Mössbauer studies on iron(II)‐substituted yeast metallothionein
- 1 August 1994
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 223 (3) , 841-845
- https://doi.org/10.1111/j.1432-1033.1994.tb19060.x
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.Keywords
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