Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1974 Dec;143(3):763–765. doi: 10.1042/bj1430763

Mössbauer effect in the `super-reduced' form of the high-potential iron–sulphur protein from Chromatium (Short Communication)

Dominic P E Dickson 1,2, Richard Cammack 1,2
PMCID: PMC1168445  PMID: 4376953

Abstract

Mössbauer-effect studies of the super-reduced form of Chromatium high-potential iron–sulphur protein indicate that the iron atoms are in a similar valency state to those in reduced ferredoxin from Clostridium pasteurianum, with possibly some inequivalence between the iron atoms within the four-iron centre. Mössbauer spectroscopy also shows magnetic differences between the four-iron centres in the two proteins.

Full text

PDF
763

Selected References

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

  1. Cammack R. "Super-reduction" of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide. Biochem Biophys Res Commun. 1973 Sep 18;54(2):548–554. doi: 10.1016/0006-291x(73)91457-5. [DOI] [PubMed] [Google Scholar]
  2. Carter C. W., Jr, Kraut J., Freer S. T., Alden R. A., Sieker L. C., Adman E., Jensen L. H. A comparison of Fe 4 S 4 clusters in high-potential iron protein and in ferredoxin. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3526–3529. doi: 10.1073/pnas.69.12.3526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dickson D. P., Johnson C. E., Cammack R., Evans M. C., Hall D. O., Rao K. K. Mössbauer effect in the high-potential iron-sulphur protein from Chromatium. Evidence for the state of the iron atoms. Biochem J. 1974 Apr;139(1):105–108. doi: 10.1042/bj1390105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Frankel R. B., Herskovitz T., Averill B. A., Holm R. H., Krusic P. J., Phillips W. D. Synthetic analogs of the active sites of iron-sulfur proteins. 8. Some electronic properties of (Fe4S4(SR)4)3-, analogs of reduced bacterial ferredoxins. Biochem Biophys Res Commun. 1974 Jun 18;58(4):974–982. doi: 10.1016/s0006-291x(74)80239-1. [DOI] [PubMed] [Google Scholar]
  5. Gersonde K., Schlaak H. E., Breitenbach M., Parak F., Eicher H., Zgorzalla W., Kalvius M. G., Mayer A. Mössbauer effect and electron spin resonance of the (iron)4-sulfur clusters of ferredoxin from Clostridium pasteurianum. Eur J Biochem. 1974 Apr 1;43(2):307–317. doi: 10.1111/j.1432-1033.1974.tb03414.x. [DOI] [PubMed] [Google Scholar]
  6. Herskovitz T., Averill B. A., Holm R. H., Ibers J. A., Phillips W. D., Weiher J. F. Structure and properties of a synthetic analogue of bacterial iron--sulfur proteins. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2437–2441. doi: 10.1073/pnas.69.9.2437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Thompson C. L., Johnson C. E., Dickson D. P., Cammack R., Hall D. O., Weser U., Rao K. K. Mössbauer effect in the eight-iron ferredoxin from Clostridium pasterurianum. Evidence for the state of the iron atoms. Biochem J. 1974 Apr;139(1):97–103. doi: 10.1042/bj1390097. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES