at Google ScholarTitle data
Baumann, Bettina ; Sticht, Heinrich ; Schärpf, Manuela ; Sutter, Martin ; Haehnel, Wolfgang ; Rösch, Paul:
Structure of Synechococcus elongatus [Fe₂-S₂] Ferredoxin in Solution.
In: Biochemistry.
Vol. 35
(1996)
Issue 39
.
- pp. 12831-12841.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi961144m
Abstract in another language
Ferredoxins of the [Fe2S2] type function in photosynthetic electron transport as essential electron acceptors of photosystem I. The solution structure of the 97 amino acid ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus was determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics calculations. The structure consists of a four-stranded parallel/ antiparallel beta-sheet, a short two-stranded antiparallel beta-sheet, and three short helices. The overall structure is similar to the structure of the ferredoxin from Anabaena. In contrast to related ferredoxins from mesophilic organisms, this thermostable protein contains a salt bridge inside a 17-amino acid hydrophobic core.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry |
| Result of work at the UBT: | Yes |
| DDC Subjects: | 500 Science > 540 Chemistry 500 Science > 570 Life sciences, biology |
| Date Deposited: | 11 Jan 2019 08:33 |
| Last Modified: | 31 Mar 2022 13:35 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/46887 |