Structure of Synechococcus elongatus [Fe2S2] Ferredoxin in Solution
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- 作者：Bettina Baumann ; Heinrich Sticht ; Manuela Schä ; rpf ; Martin Sutter ; Wolfgang Haehnel ; and Paul Rö ; sch
- 刊名：Biochemistry
- 出版年：1996
- 出版时间：October 1, 1996
- 年：1996
- 卷：35
- 期：39
- 页码：12831 - 12841
- 全文大小：635K
- 年卷期：v.35,no.39(October 1, 1996)
- ISSN：1520-4995
文摘
Ferredoxins of the [Fe2S2] type functionin photosynthetic electron transport as essential electronacceptors of photosystem I. The solution structure of the 97 aminoacid ferredoxin from the thermophiliccyanobacterium Synechococcus elongatus was determined bynuclear magnetic resonance spectroscopyand restrained molecular dynamics calculations. The structureconsists of a four-stranded parallel/antiparallel 
-sheet, a short two-stranded antiparallel -sheet, andthree short helices. The overall structureis similar to the structure of the ferredoxin from Anabaena.In contrast to related ferredoxins frommesophilic organisms, this thermostable protein contains a salt bridgeinside a 17-amino acid hydrophobiccore.
-sheet, a short two-stranded antiparallel -sheet, andthree short helices. The overall structureis similar to the structure of the ferredoxin from Anabaena.In contrast to related ferredoxins frommesophilic organisms, this thermostable protein contains a salt bridgeinside a 17-amino acid hydrophobiccore.