Rieske protein

Rieske protein

Symbol = Rieske
Name =

width =260
caption =Mitochondrial cytochrome bc1 complex. (PDB|1bcc)
Pfam= PF00355
InterPro= IPR005806
SCOP = 1rie
TCDB = 3.E.2
OPM family=
OPM protein= 1q90
PDB=PDB3|1ww9A:28-131 PDB3|1z01E:43-146 PDB3|1z03C:43-146PDB3|1z02A:43-146 PDB3|1fqtA:2-96 PDB3|1vckA:4-98PDB3|1sjgA:2-96 PDB3|1vm9A:2-96 PDB3|1wqlA:58-165PDB3|1uliA:55-148 PDB3|1uljC:55-148 PDB3|2bmqA:36-137PDB3|2bmoA:36-137 PDB3|2bmrA:36-137 PDB3|1o7nA:38-139PDB3|1o7wA:38-139 PDB3|1eg9A:38-139 PDB3|1o7hA:38-139PDB3|1ndoC:38-139 PDB3|1o7pA:38-139 PDB3|1uuvA:38-139PDB3|1o7mA:38-139 PDB3|1uuwA:38-139 PDB3|1o7gA:38-139PDB3|2b1xA:45-158 PDB3|2b24A:45-158 PDB3|1rfs :137-206PDB3|1q90C:113-182 PDB3|1vf5Q:64-158 PDB3|2d2cQ:64-158PDB3|1g8kH:47-110 PDB3|1g8jD:47-110 PDB3|1nykA:89-185PDB3|1jm1A:96-204 PDB3|1kyoP:116-208 PDB3|1p84E:116-208PDB3|1kb9E:116-208 PDB3|1nu1E:174-266 PDB3|1rie :174-266PDB3|1ntzE:174-266 PDB3|1sqqE:174-266 PDB3|1l0nE:174-266PDB3|1be3E:174-266 PDB3|1sqvE:174-266 PDB3|1sqpE:174-266PDB3|1l0lE:174-266 PDB3|1bccE:174-266 PDB3|1ntmE:174-266PDB3|1ntkE:174-266 PDB3|1sqbE:174-266 PDB3|1sqxE:174-266

Rieske protein is a iron-sulfur protein (ISP) component of cytochrome "bc"1 complex which was first discovered and isolated by John S. Rieske and co-workers in 1964.

Biological function

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 synthesiscite journal |author=Harnisch U, Weiss H, Sebald W |title=The primary structure of the iron-sulfur subunit of ubiquinol-cytochrome c reductase from Neurospora, determined by cDNA and gene sequencing |journal=Eur. J. Biochem. |volume=149 |issue=1 |pages=95–99 |year=1985 |pmid=2986972 |doi=10.1111/j.1432-1033.1985.tb08898.x] cite journal |author=Sebald W, Gabellini N |title=Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c1 |journal=Eur. J. Biochem. |volume=154 |issue=3 |pages=569–579 |year=1986 |pmid=3004982 |doi=10.1111/j.1432-1033.1986.tb09437.x] . 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 clustercite journal |author=Ludwig B, Kurowski B |title=The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits |journal=J. Biol. Chem. |volume=262 |issue=28 |pages=13805–13811 |year=1987 |pmid=2820981] .The mitochondrial form also includes six other subunits that do not possess redox centres. Plastoquinone-plastocyanin reductase (b6f complex), present in cyanobacteria and the chloroplasts of plants, catalyses the oxidoreduction of plastoquinol and cytochrome f. This complex, which is functionally similar to ubiquinol-cytochrome c reductase, comprises cytochrome b6, cytochrome f and Rieske subunitscite journal |author=Madueno F, Napier JA, Cejudo FJ, Gray JC |title=Import and processing of the precursor of the Rieske FeS protein of tobacco chloroplasts |journal=Plant Mol. Biol. |volume=20 |issue=2 |pages=289–299 |year=1992 |pmid=1391772 |doi=10.1007/BF00014496] .

The Rieske subunit acts by binding either a ubiquinol or plastoquinol anion, transferring an electron to the 2Fe-2S cluster, then releasing the electron to the cytochrome c or cytochrome f haem iron. The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion while the other Fe ion is coordinated by two conserved histidines. The 2Fe-2S cluster is bound in the highly conserved C-terminal region of the Rieske subunit.

Rieske protein family

The homologues of the Rieske proteins include ISP components of cytochrome "b"6"f" complex, aromatic-ring-hydroxylating dioxygenases (phthalate dioxygenase, benzene, napthalene and toluene 1,2-dioxygenases) and arsenite oxidase (EC [http://www.expasy.org/cgi-bin/get-enzyme-entry?] ). Comparison of amino acid sequences has revealed the following consensus sequence:: Cys-Xaa-His-(Xaa)15–17-Cys-Xaa-Xaa-His

3D structure

The crystal structures of a number of Rieske proteins are known. The overall fold, comprising two subdomains, is dominated by antiparallel β-structure and contains the only α-helix. The smaller "cluster-binding" subdomains in mitochondrial and chloroplast proteins are virtually identical, whereas the large subdomains are substantially different in spite of a common folding topology. The [Fe2S2] cluster-binding subdomains have the topology of an incomplete antiparallel β-barrel. One iron atom of the Rieske [Fe2S2] cluster is coordinated by two cysteine residues and the other is coordinated by two histidine residues through the Nδ atoms. The ligands coordinating the cluster originate from two loops; each loop contributes one Cys and one His.


*Rieske iron-sulphur protein, C-terminal InterPro|IPR005805
*Arsenite oxidase, small subunit InterPro|IPR014067

Human proteins containing this domain



Further reading

*Structure of a water soluble fragment of the 'Rieske' iron- sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution. Iwata S, Saynovits M, Link TA, Michel H Structure 1996;4:567-579. PMID|8736555
*Functional analysis in yeast of cDNA coding for the mitochondrial Rieske iron-sulfur protein of higher plants. Huang JT, Struck F, Matzinger DF, Levings CS; Proc Natl Acad Sci U S A 1991;88:10716-10720. PMID|1961737
*The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex. Brandt U, Yu L, Yu CA, Trumpower BL; J Biol Chem 1993;268:8387-8390. PMID|8386158

External links

* - X-ray structure of Rieske protein (water-soluble fragment) of the bovine mitochondrial cytochrome "bc"1 complex
* - X-ray structure of Rieske protein (water-soluble fragment) of the spinach chloroplast cytochrome "b"6" f"complex
* - X-ray structure of Rieske-type ferredoxin associated with biphenyl dioxygenase from "Burkholderia cepacia"
* - X-ray structure of Rieske subunit of arsenite oxidase from "Alcaligenes faecalis"
* - InterPro entry for Rieske [2Fe-2S] region

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