Reconstitution of an Iron-Sulfur Cluster with Bound Sulfur : A Possible Source of Acid-Labile Sulfur in Biological Systems

概要

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The reconstitution of the iron-sulfur cluster of spinach ferredoxin was examined in vitro using low and high molecular bound sulfur components as sulfur donors. Bound sulfur was rapidly converted to acid-labile sulfur to form an iron-sulfur center in the presence of dihydrolipoate and iron. Reconstitution yields of above 95% were obtained with cystine trisulfide (CT, 0.25mM) and sulfur-bound albumin (SBA, 1.0mM) at 37℃, pH 7.3,following 60min incubation. Spectroscopic features and biological activity of the reconstituted ferredoxin were identical to those of the native holo-protein. The acid-labile sulfur content found in the isolated reconstituted ferredoxin was 2atoms/mol protein, similar to the theoretical value. A possible role for bound sulfur in mammalian cells is indicated and discussed.
社団法人日本薬学会の論文
1995-08-15