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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Nov;75(11):5273–5275. doi: 10.1073/pnas.75.11.5273

Cluster characterization in iron-sulfur proteins by magnetic circular dichroism.

P J Stephens, A J Thomson, T A Keiderling, J Rawlings, K K Rao, D O Hall
PMCID: PMC392944  PMID: 281679

Abstract

We report magnetic circular dichroism (MCD) spectra of 4-Fe iron-sulfur clusters in the iron-sulfur proteins Chromatium high-potential iron protein (HIPIP), Bacillus stearothermophilus ferredoxin and Clostridium pasteurianum ferredoxin. The MCD is found to vary significantly with cluster oxidation state but is relatively insensitive to the nature of the protein. The spectra obtained are compared with the corresponding spectra of iron-sulfur proteins containing 2-Fe clusters. It is concluded that MCD is useful for the characterization of iron-sulfur cluster type and oxidation state in iron-sulfur proteins and is superior for this purpose to absorption and natural circular dichroism spectroscopy.

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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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