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Mössbauer studies on yeast metallothionein (1994)

Ding, X. -Q. ; Bill, E. ; Trautwein, A. X. ; [et al.]

Springer

Hyperfine interactions 91 (1994), S. 791-795

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ISSN: 1572-9540

Source: Springer Online Journal Archives 1860-2000

Topics: Physics

Notes: Abstract 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02064608

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