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| Mitochondrial cytochrome bc1 complex. (PDB 1bcc) | ||
| Identifiers | ||
|---|---|---|
| Symbol | Rieske | |
| Pfam | PF00355 | |
| InterPro | IPR005806 | |
| PROSITE | PDOC00177 | |
| SCOP | 1rie | |
| TCDB | 3.E.2 | |
| OPM protein | 1q90 | |
| Available PDB structures:
1ww9A:28-131 1z01E:43-146 1z03C:43-146 1z02A:43-146 1fqtA:2-96 1vckA:4-98 1sjgA:2-96 1vm9A:2-96 1wqlA:58-165 1uliA:55-148 1uljC:55-148 2bmqA:36-137 2bmoA:36-137 2bmrA:36-137 1o7nA:38-139 1o7wA:38-139 1eg9A:38-139 1o7hA:38-139 1ndoC:38-139 1o7pA:38-139 1uuvA:38-139 1o7mA:38-139 1uuwA:38-139 1o7gA:38-139 2b1xA:45-158 2b24A:45-158 1rfs :137-206 1q90C:113-182 1vf5Q:64-158 2d2cQ:64-158 1g8kH:47-110 1g8jD:47-110 1nykA:89-185 1jm1A:96-204 1kyoP:116-208 1p84E:116-208 1kb9E:116-208 1nu1E:174-266 1rie :174-266 1ntzE:174-266 1sqqE:174-266 1l0nE:174-266 1be3E:174-266 1sqvE:174-266 1sqpE:174-266 1l0lE:174-266 1bccE:174-266 1ntmE:174-266 1ntkE:174-266 1sqbE:174-266 1sqxE:174-266 |
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Rieske protein is a iron-sulfur protein (ISP) component of cytochrome bc1 complex and the cytochrome b6f complex which was first discovered and isolated by John S. Rieske and co-workers in 1964.[1]
Contents |
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 synthesis.[2][3]
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.[4] 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 subunits.[5]
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.[2][5] The reduction of the Rieske center increases the affinity of the subunit by several orders of magnitude, stabilizing the semiquinone radical at the Q(P) site.[6] 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 b6f complex, aromatic-ring-hydroxylating dioxygenases (phthalate dioxygenase, benzene, napthalene and toluene 1,2-dioxygenases) and arsenite oxidase (EC 1.20.98.1). 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.
Subfamilies
Human proteins containing this domain
AIFM3; RFESD; UQCRFS1;
References
- ^ Rieske JS, Maclennan DH, Coleman, R (1964). "Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain". Biochem. Biophys. Res. Commun 15: 338–344. doi:.
- ^ a b Harnisch U, Weiss H, Sebald W (May 1985). "The primary structure of the iron-sulfur subunit of ubiquinol-cytochrome c reductase from Neurospora, determined by cDNA and gene sequencing". Eur. J. Biochem. 149 (1): 95–9. doi:. PMID 2986972.
- ^ Gabellini N, Sebald W (February 1986). "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". Eur. J. Biochem. 154 (3): 569–79. doi:. PMID 3004982.
- ^ Kurowski B, Ludwig B (October 1987). "The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits". J. Biol. Chem. 262 (28): 13805–11. PMID 2820981.
- ^ a b Madueño F, Napier JA, Cejudo FJ, Gray JC (October 1992). "Import and processing of the precursor of the Rieske FeS protein of tobacco chloroplasts". Plant Mol. Biol. 20 (2): 289–99. doi:. PMID 1391772.
- ^ Link TA (July 1997). "The role of the 'Rieske' iron sulfur protein in the hydroquinone oxidation (Q(P)) site of the cytochrome bc1 complex. The 'proton-gated affinity change' mechanism". FEBS Lett. 412 (2): 257–64. doi:. PMID 9256231.
Further reading
- Iwata S, Saynovits M, Link TA, Michel H (May 1996). "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". Structure 4 (5): 567–79. doi:. PMID 8736555.
- Huang JT, Struck F, Matzinger DF, Levings CS (December 1991). "Functional analysis in yeast of cDNA coding for the mitochondrial Rieske iron-sulfur protein of higher plants". Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10716–20. doi:. PMID 1961737.
- Brandt U, Yu L, Yu CA, Trumpower BL (April 1993). "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". J. Biol. Chem. 268 (12): 8387–90. PMID 8386158.
- Ferraro, D.J., Gakhar, L. and Ramaswamy, S. (2005). "Rieske business: structure-function of Rieske non-heme oxygenases". Biochem. Biophys. Res. Commun. 338: 175–190. doi:. PMID 16168954.
- Mason, J.R. and Cammack, R. (1992). "The electron-transport proteins of hydroxylating bacterial dioxygenases". Annu. Rev. Microbiol. 46: 277–305. doi:. PMID 1444257.
- Schmidt, C.L. (2004). "Rieske iron-sulfur proteins from extremophilic organisms". J. Bioenerg. Biomembr. 36: 107–113. doi:. PMID 15168614.
- Schneider, D. and Schmidt, C.L. (2005). "Multiple Rieske proteins in prokaryotes: where and why?". Biochim. Biophys. Acta 1710: 1–12. PMID 16271700.
External links
- PDB 1RIE - X-ray structure of Rieske protein (water-soluble fragment) of the bovine mitochondrial cytochrome bc1 complex
- PDB 1RFS - X-ray structure of Rieske protein (water-soluble fragment) of the spinach chloroplast cytochrome b6 fcomplex
- PDB 1FQT - X-ray structure of Rieske-type ferredoxin associated with biphenyl dioxygenase from Burkholderia cepacia
- PDB 1G8J - X-ray structure of Rieske subunit of arsenite oxidase from Alcaligenes faecalis
- IPR005806 - InterPro entry for Rieske [2Fe-2S] region
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