TY - JOUR
T1 - Mössbauer studies on iron(II)‐substituted yeast metallothionein
AU - DING, Xiao‐Qi ‐Q
AU - BILL, Eckhard
AU - TRAUTWEIN, Alfred Xaver
AU - HARTMANN, Hans‐Jürgen ‐J
AU - WESER, Ulrich
PY - 1994/8/1
Y1 - 1994/8/1
N2 - 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 non‐interacting, with each individual iron(II) behaving like iron(II) in reduced rubredoxin.
AB - 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 non‐interacting, with each individual iron(II) behaving like iron(II) in reduced rubredoxin.
UR - http://www.scopus.com/inward/record.url?scp=0028168398&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1994.tb19060.x
DO - 10.1111/j.1432-1033.1994.tb19060.x
M3 - Journal articles
C2 - 8055961
AN - SCOPUS:0028168398
SN - 0014-2956
VL - 223
SP - 841
EP - 845
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -
