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. 1990 Jan;87(2):598–602. doi: 10.1073/pnas.87.2.598

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement.

A E Martín 1, B K Burgess 1, C D Stout 1, V L Cash 1, D R Dean 1, G M Jensen 1, P J Stephens 1
PMCID: PMC53312  PMID: 2153958

Abstract

Azotobacter vinelandii ferredoxin I is a small protein that contains one [4Fe-4S] cluster and one [3Fe-4S] cluster. Recently the x-ray crystal structure has been redetermined and the fdxA gene, which encodes the protein, has been cloned and sequenced. Here we report the site-directed mutation of Cys-20, which is a ligand of the [4Fe-4S] cluster in the native protein, to alanine and the characterization of the protein product by x-ray crystallographic and spectroscopic methods. The data show that the mutant protein again contains one [4Fe-4S] cluster and one [3Fe-4S] cluster. The new [4Fe-4S] cluster obtains its fourth ligand from Cys-24, a free cysteine in the native structure. The formation of this [4Fe-4S] cluster drives rearrangement of the protein structure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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