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

Zach Adam; Richard Malkin

doi:10.1016/0014-5793(87)81132-8

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 journal › Article › peer-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 language	English
Pages (from-to)	67-71
Number of pages	5
Journal	FEBS Letters
Volume	225
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(87)81132-8
State	Published - 10 Dec 1987
Externally published	Yes

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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10.1016/0014-5793(87)81132-8

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title = "Reconstitution of isolated Rieske Fe-S protein into a Rieske-depleted cytochrome b6-ƒ complex",

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.",

keywords = "Cytochrome b-f{hook}, Reconstitution, Rieske Fe-S protein",

author = "Zach Adam and Richard Malkin",

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

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doi = "10.1016/0014-5793(87)81132-8",

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T1 - Reconstitution of isolated Rieske Fe-S protein into a Rieske-depleted cytochrome b6-ƒ complex

AU - Adam, Zach

AU - Malkin, Richard

N1 - Funding Information: This work was supported in part by a grant from the National Institutes of Health.

PY - 1987/12/10

Y1 - 1987/12/10

N2 - 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.

AB - 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.

KW - Cytochrome b-f{hook}

KW - Reconstitution

KW - Rieske Fe-S protein

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SN - 0014-5793

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JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

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

Abstract

Bibliographical note

Keywords

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