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ESR studies on iron‐sulfur clusters of complex II in Ascaris suum mitochondria which exhibits strong fumarate reductase activity
Author(s) -
Hata-Tanaka Akiko,
Kita Kiyoshi,
Furushima Rieko,
Oya Hiroshi,
Itoh Shigeru
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81012-3
Subject(s) - fumarate reductase , ascaris suum , dithionite , chemistry , succinate dehydrogenase , reductase , electron paramagnetic resonance , sulfur , iron–sulfur cluster , cluster (spacecraft) , mitochondrion , desulfovibrio , crystallography , biochemistry , stereochemistry , enzyme , nuclear magnetic resonance , sulfate , biology , organic chemistry , zoology , physics , computer science , programming language , helminths
Complex II of Ascaris suum mitochondria, which functions as fumarate reductase in physiological conditions, contains three types of iron‐sulfur clusters. These correspond to clusters S‐1, S‐2 and S‐3 and are distinguishable by low‐temperature ESR studies. Cluster S‐1 is reduced by succinate, giving ESR signals with g z , g y and g x values at 2.033, 1.939 and 1.920. The existence of cluster S‐2 is suggested by an enhancement of the S‐1 spin relaxation induced upon reduction of S‐2 by dithionite. Cluster S‐3 is ESR detectable under air‐oxidized conditions and gives a strong signal at g = 2.025. Cluster S‐3 was only partially reduced even with an excess amount of sodium succinate, which is a common characteristic of fumarate reductase but this is not seen in the mitochondrial complex II.