Pathways & interactions
Rieske [2Fe-2S] iron-sulphur domain superfamily (IPR036922)
Short name: Rieske_2Fe-2S_sf
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit (IPR001663)
- Rieske iron-sulphur protein, C-terminal (IPR005805)
- Ubiquinol-cytochrome c reductase, iron-sulphur subunit (IPR006317)
- MocE Rieske [2Fe-2S] (IPR012747)
- Rieske-like [2Fe-2S] domain, NirD-type (IPR012748)
- Arsenite oxidase, small subunit (IPR014067)
- Rieske iron-sulphur protein (IPR014349)
- Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site (IPR015881)
- Rieske iron-sulphur protein SoxL2 (IPR017586)
- Nitrite reductase (NADH) small subunit (IPR017881)
- Rieske [2Fe-2S] iron-sulphur domain (IPR017941)
- 3-phenylpropionate/cinnamic acid dioxygenase, ferredoxin subunit (IPR023739)
- Cytochrome b6-f complex iron-sulfur subunit (IPR023960)
- Aminopyrrolnitrin oxygenase PrnD, Rieske domain (IPR037338)
- Cytidine monophosphate-N-acetylneuraminic acid hydroxylase, Rieske domain (IPR037339)
- YhfW, C-terminal Rieske domain (IPR038010)
There are multiple types of iron-sulphur clusters which are grouped into three main categories based on their atomic content: [2Fe-2S], [3Fe-4S], [4Fe-4S] (see PDOC00176), and other hybrid or mixed metal types. Two general types of [2Fe-2S] clusters are known and they differ in their coordinating residues. The ferredoxin-type [2Fe-2S] clusters are coordinated to the protein by four cysteine residues (see PDOC00175). The Rieske-type [2Fe-2S] cluster is coordinated to its protein by two cysteine residues and two histidine residues [PMID: 16168954, PMID: 16271700].
The structure of several Rieske domains has been solved [PMID: 8736555]. It contains three layers of antiparallel beta sheets forming two beta sandwiches. Both beta sandwiches share the central sheet 2. The metal-binding site is at the top of the beta sandwich formed by the sheets 2 and 3. The Fe1 iron of the Rieske cluster is coordinated by two cysteines while the other iron Fe2 is coordinated by two histidines. Two inorganic sulphide ions bridge the two iron ions forming a flat, rhombic cluster.
Rieske-type iron-sulphur clusters are common to electron transfer chains of mitochondria and chloroplast and to non-haem iron oxygenase systems:
- The Rieske protein of the Ubiquinol-cytochrome c reductase (EC:126.96.36.199) (also known as the bc1 complex or complex III), a complex of the electron transport chains of mitochondria and of some aerobic prokaryotes; it catalyses the oxidoreduction of ubiquinol and cytochrome c.
- The Rieske protein of chloroplastic plastoquinone-plastocyanin reductase (EC:188.8.131.52) (also known as the b6f complex). It is functionally similar to the bc1 complex and catalyses the oxidoreduction of plastoquinol and cytochrome f.
- Bacterial naphthalene 1,2-dioxygenase subunit alpha, a component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyses the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol.
- Bacterial 3-phenylpropionate dioxygenase ferredoxin subunit.
- Bacterial toluene monoxygenase.
- Bacterial biphenyl dioxygenase.