Abstract
Iron–sulfur clusters constitute a group of cofactors found in many proteins that play key roles in an exceptionally wide range of metabolic processes. The chemical reactivity of iron–sulfur clusters means that they can be particularly prone to damage when removed from the protective environment of the cell. In general, the key to obtaining an intact, biologically active iron–sulfur cluster-containing protein is to maintain a strictly anaerobic environment throughout the entire process of protein purification and analysis. For many proteins, particularly those with more labile clusters, it is essential.
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Acknowledgements
This work has been supported by a series of grants from the BBSRC, held jointly between UEA and the University of Sheffield, over several years.
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Crack, J.C., Green, J., Thomson, A.J., Le Brun, N.E. (2014). Techniques for the Production, Isolation, and Analysis of Iron–Sulfur Proteins. In: Fontecilla-Camps, J., Nicolet, Y. (eds) Metalloproteins. Methods in Molecular Biology, vol 1122. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-794-5_4
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DOI: https://doi.org/10.1007/978-1-62703-794-5_4
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