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

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Physik

Eberhard Karls Universität Tübingen

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.

Originalsprache	Englisch
Zeitschrift	Hyperfine Interactions
Jahrgang	91
Ausgabenummer	1
Seiten (von - bis)	791-795
Seitenumfang	5
ISSN	0304-3834
DOIs	https://doi.org/10.1007/BF02064608
Publikationsstatus	Veröffentlicht - 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.",

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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.

UR - https://www.scopus.com/pages/publications/34249764436

U2 - 10.1007/BF02064608

DO - 10.1007/BF02064608

M3 - Journal articles

AN - SCOPUS:34249764436

SN - 0304-3834

VL - 91

SP - 791

EP - 795

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1

ER -

Mössbauer studies on yeast metallothionein

Abstract

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