Reconstitution of isolated Rieske Fe-S protein into a Rieske-depleted cytochrome b6-ƒ complex

Zach Adam*, Richard Malkin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The Rieske Fe-S protein can be isolated from the cytochrome b6-f{hook} complex by means of chromatography on a hydroxyapatite column in the presence of detergent. Depletion of the cytochrome complex from the Rieske protein results in the loss of oxidoreductase activity, as well as the ability to reduce cytochrome b6. The Rieske Fe-S protein can be reconstituted into the Rieske-depleted complex by removal of the Triton X-100 molecules associated with the protein fractions, and their substitution by lipids. Upon reconstitution the complex is reactivated, and the role of the Rieske Fe-S protein in the reduction of both plastocyanin and cytochrome b6 can be demonstrated.

Original languageAmerican English
Pages (from-to)67-71
Number of pages5
JournalFEBS Letters
Volume225
Issue number1-2
DOIs
StatePublished - 10 Dec 1987
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported in part by a grant from the National Institutes of Health.

Keywords

  • Cytochrome b-f{hook}
  • Reconstitution
  • Rieske Fe-S protein

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