Rieske protein

Rieske Protein

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Rieske protein

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Rieske proteins are iron-sulfur protein (ISP) components of cytochrome bc<sub>1</sub> complexes and cytochrome b<sub>6</sub>f complexes which were first discovered and isolated by John S. Rieske and co-workers in 1964.

Biological function (in oxidative phosphorylation systems)

Ubiquinol-cytochrome-c reductase (also known as bc1 complex or complex III) is an enzyme complex of bacterial and mitochondrial oxidative phosphorylation systems. It catalyses the oxidoreduction of the mobile redox components ubiquinol and cytochrome c, generating an electrochemical potential, which is linked to ATP synthesis.

The complex consists of three subunits in most bacteria, and nine in mitochondria: both bacterial and mitochondrial complexes contain cytochrome b and cytochrome c1 subunits, and an iron-sulphur 'Rieske' subunit, which contains a high potential 2Fe-2S cluster. The mitochondrial form also includes six other subunits that do not possess...
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