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Structure-function relationship of [2Fe-2S] ferredoxins and design of a model molecule.

Authors
Type
Published Article
Journal
Biosystems
0303-2647
Publisher
Elsevier
Publication Date
Volume
15
Issue
3
Pages
243–257
Identifiers
PMID: 7139087
Source
Medline

Abstract

[2Fe-2S] ferredoxins isolated from various plants and algae comprise 93-99 amino acid residues and resemble each other not only in sequences, but also in physiological functions. One of them isolated from Spirulina platensis was subjected to X-ray analysis and its three dimensional structure is now known. [2Fe-2S] ferredoxins of a different type are found in halobacteria and comprise 128 amino acid residues. Both types of the [2Fe-2S] ferredoxins exhibit low redox potentials. By comparing the amino acid sequences of 28 [2Fe-2S] ferredoxins and the tertiary structure of S. platensis ferredoxin we predicted a common three-dimensional structure to the [2Fe-2S] ferredoxins and proposed a molecular surface area to be interacting with FNR. An artificial small molecule composed of 20 amino acid residues is designed on the basis of the tertiary structure of S. platensis ferredoxin. The amino acid sequence was predicted to be Pro-Tyr-Ser-Cys-Arg-Ala-Gly-Ala-Cys-Ser-Thr-Cys-Ala-Gyl-Pro-Leu-Leu-Thr Cys-Val which should have a [2Fe-2S] cluster with a low redox potential.

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