首页    期刊浏览 2025年02月26日 星期三
登录注册

文章基本信息

  • 标题:Iron-sulfur proteins: spin-coupling model for three-iron clusters
  • 本地全文:下载
  • 作者:T A Kent ; B H Huynh ; E Münck
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1980
  • 卷号:77
  • 期号:11
  • 页码:6574-6576
  • DOI:10.1073/pnas.77.11.6574
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Recent Mossbauer and EPR studies of two ferredoxins and of aconitase have given evidence for a three-iron cluster, probably of a [3Fe-3S] type. The studies of the oxidized EPR-active centers have shown that the three iron sites are characterized by significantly different magnetic hyperfine coupling constants. For the ferredoxin from Azotobacter vinelandii, for instance, we have observed A1 = -41 MHz, A2 = +18 MHz, and [A3] = 5 MHz. We demonstrate here that the magnetic properties of the clusters can be explained with a simple model of three high-spin ferric ions (S = 5/2) exchange-coupled to a system spin S = 1/2. The model assumes isotropic exchange and different couplings between the iron sites. The results show that the three sites have intrinsic hyperfine interactions similar to those of ferric rubredoxin; the differences in the observed interactions reflect the geometrical features of spin coupling. Furthermore, the three exchange coupling constants are equal within a factor of 2. This implies that the three-iron cluster is a single covalently linked structure and should not be considered as a [2Fe-2S] cluster weakly coupled to a third iron atom.
国家哲学社会科学文献中心版权所有