Affiliation:
1. Department of Chemistry, Duquesne University, Pittsburgh, Pa. 15219, U.S.A.
Abstract
Aconitase activated with Fe2+, cysteine and ascorbate incorporates 1 g-atom of Fe2+/mol. Loss of this Fe2+ by transfer to ferrozine, a Fe2+ chelator, results in loss of activity. Ascorbate increases the rate of transfer of the essential Fe2+ whereas citrate retards the rate of transfer. Transfer of Fe2+ from inactive aconitase, 2 g-atoms of Fe/mol, can be accomplished in the presence of urea and ascorbate. The correlation of activity with the presence of an added g-atom of Fe2+/mol leads to the conclusion that active aconitase has only one active site per mol.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
41 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献