Conversion of Clostridium pasteurianum rubredoxin into a four-iron ferredoxin
- 1 January 1979
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Chemical Communications
- No. 1,p. 20-21
- https://doi.org/10.1039/c39790000020
Abstract
Denatured C. pasteurianum rubredoxin in 90% aqueous dimethyl sulphoxide is converted, by addition of sodium sulphide, iron(II) chloride, and iron(III) chloride, into a four-iron ferredoxin, which is partially reconverted into the rubredoxin on renaturation of the protein by dilution with water.This publication has 3 references indexed in Scilit:
- Synthetic analogs of the active sites of iron-sulfur proteins. 15. Comparative polarographic potentials of the [Fe4S4(SR)4]2-,3- and Clostridium pasteurianum ferredoxin redox couplesJournal of the American Chemical Society, 1977
- Synthetic analogs of the active sites of iron-sulfur proteins. 14. Synthesis, properties, and structures of bis(o-xylyl-.alpha.,.alpha.'-dithiolato)ferrate(II,III) anions, analogs of oxidized and reduced rubredoxin sitesJournal of the American Chemical Society, 1977
- Direct formation of peptide analogues of rubredoxins and four-iron ferredoxins from their componentsJournal of the Chemical Society, Chemical Communications, 1977