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. 1969 Aug;63(4):1234–1238. doi: 10.1073/pnas.63.4.1234

MÖSSBAUER SPECTROSCOPY OF THE IRON-SULFUR PROTEINS*

C E Johnson 1,2,3, R C Bray 1,2,3, R Cammack 1,2,3, D O Hall 1,2,3
PMCID: PMC223455  PMID: 5260925

Abstract

The Mössbauer spectra of 57Fe in two plant ferredoxins (from spinach and Euglena) and in xanthine oxidase have been measured at a series of temperatures and magnetic fields, and are found to be similar in all three proteins. In the oxidized state the iron is nonmagnetic. In the reduced state, the iron nuclei show magnetic hyperfine interaction with an electron spin S of ½, producing an effective field of about 180 kG at the nuclei.

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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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