Mössbauer studies on yeast metallothionein

X. Q. Ding; E. Bill; A. X. Trautwein; H. J. Hartmann; U. Weser

doi:10.1007/BF02064608

Mössbauer studies on yeast metallothionein

X. Q. Ding^*, E. Bill, A. X. Trautwein, H. J. Hartmann, U. Weser

^*Corresponding author for this work

Institute of Physics

University of Tubingen

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.

Original language	English
Journal	Hyperfine Interactions
Volume	91
Issue number	1
Pages (from-to)	791-795
Number of pages	5
ISSN	0304-3834
DOIs	https://doi.org/10.1007/BF02064608
Publication status	Published - 01.12.1994

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abstract = "Iron-substituted yeast metallothionein, Fe(II)-yeast-MT, has been studied by M{\"o}ssbauer 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.",

author = "Ding, {X. Q.} and E. Bill and Trautwein, {A. X.} and Hartmann, {H. J.} and U. Weser",

year = "1994",

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doi = "10.1007/BF02064608",

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T1 - Mössbauer studies on yeast metallothionein

AU - Ding, X. Q.

AU - Bill, E.

AU - Trautwein, A. X.

AU - Hartmann, H. J.

AU - Weser, U.

PY - 1994/12/1

Y1 - 1994/12/1

N2 - 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.

AB - 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.

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M3 - Journal articles

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SN - 0304-3834

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SP - 791

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JO - Hyperfine Interactions

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IS - 1

ER -

Mössbauer studies on yeast metallothionein

Abstract

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