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Reconstitution of isolated Rieske Fe‐S protein into a Rieske‐depleted cytochrome b 6 ‐ƒ complex
Author(s) -
Adam Zach,
Malkin Richard
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81132-8
Subject(s) - plastocyanin , cytochrome , chemistry , coenzyme q – cytochrome c reductase , cytochrome c , cytochrome f , cytochrome b , oxidoreductase , biochemistry , enzyme , mitochondrion , chloroplast , gene , mitochondrial dna , photosystem i
The Rieske Fe‐S protein can be isolated from the cytochrome b 6 ‐ƒ 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 b 6 . 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 b 6 can be demonstrated.