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Characterization of a novel ferredoxin with N-terminal extension from Clostridium acetobutylicum ATCC 824

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Abstract

A gene (CAC2657) encoding a ferredoxin (EFR1) from the strictly anaerobic soil bacterium Clostridium acetobutylicum was cloned and expressed in Escherichia coli. The ferredoxin gene encodes a polypeptide of 27 kDa that incorporates 2[4Fe–4S] clusters. An extended N-terminal region of 187 amino acid (aa) residues precedes ferredoxin domain. The EFR1 expressed in E. coli is a trimeric protein. The iron and sulfur content of the reconstituted protein agrees with that expected of a trimeric form of the protein. The ferredoxin domain of EFR1 is closely related to ferredoxin of C. pasteurianum; and can be fitted to the X-ray crystal structure with a root mean square deviation of 0.62 As for the Cα atoms of the generated 3D simulation model. In cultures of C. acetobutylicum the efr1 gene shows higher relative expression on induction with Trinitrotoluene (TNT) compared to that from uninduced control cultures.

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Acknowledgements

This material is based upon work supported by the US Army Research Office DOD ARMY W911NF-04-1-0179. We would like to thank Dr. M. S. Cates for assistance with the structure modeling.

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  1. Department of Biochemistry and Cell Biology MS-140, Rice University, Houston, TX, 77005-1892, USA

    Razia Kutty & George N. Bennett

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  1. Razia Kutty
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  2. George N. Bennett
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Correspondence to George N. Bennett.

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Kutty, R., Bennett, G.N. Characterization of a novel ferredoxin with N-terminal extension from Clostridium acetobutylicum ATCC 824. Arch Microbiol 187, 161–169 (2007). https://doi.org/10.1007/s00203-006-0184-7

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  • DOI: https://doi.org/10.1007/s00203-006-0184-7

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