Rieske protein: Difference between revisions

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{{PDB3|2i7f}}
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'''Rieske protein''' is a [[iron-sulfur protein]] (ISP) component of [[cytochrome bc1 complex|cytochrome ''bc''<sub>1</sub> complex]] and the [[cytochrome b6f complex|cytochrome b<sub>6</sub>f complex]] which was first discovered and isolated by John S. Rieske and co-workers in 1964.<ref name="Rieske_1964">{{cite journal | author = Rieske JS, Maclennan DH, Coleman, R | title = Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain | journal = Biochem. Biophys. Res. Commun | volume = 15 | issue = | pages = 338–344 | year = 1964 | month = | doi = 10.1016/0006-291X(64)90171-8| url = | issn = }}</ref>. It is a unique [2Fe-2S] cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria.
'''Rieske proteins''' are [[iron-sulfur protein]] (ISP) components of [[cytochrome bc1 complex|cytochrome ''bc''<sub>1</sub> complexes]] and [[cytochrome b6f complex|cytochrome b<sub>6</sub>f complexes]] which were first discovered and isolated by John S. Rieske and co-workers in 1964.<ref name="Rieske_1964">{{cite journal | author = Rieske JS, Maclennan DH, Coleman, R | title = Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain | journal = Biochem. Biophys. Res. Commun | volume = 15 | issue = | pages = 338–344 | year = 1964 | month = | doi = 10.1016/0006-291X(64)90171-8| url = | issn = }}</ref>. It is a unique [2Fe-2S] cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria with widely ranging electron reduction potentials from -150 to +400 mV<ref name="Brown_2008">{{cite journal | author=Brown, E.N. and Friemann, R. and Karlsson, A. and Parales, J.V. and Couture, M.M. and Eltis, L.D. and Ramaswamy, S. | title=Determining Rieske cluster reduction potentials | journal=J.Biol.Inorg.Chem. | year=2008 | volume=13 | pages=1301-1313 | pmid=18719951 | doi=10.1007/s00775-008-0413-4}}</ref>.


== Biological function ==
== 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.<ref name="pmid2986972">{{cite 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 = 95–9 | year = 1985 | month = May | pmid = 2986972 | doi = 10.1111/j.1432-1033.1985.tb08898.x| url = | issn = }}</ref><ref name="pmid3004982">{{cite journal | author = Gabellini N, Sebald W | 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 = 569–79 | year = 1986 | month = February | pmid = 3004982 | doi = 10.1111/j.1432-1033.1986.tb09437.x| url = | issn = }}</ref>
[[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.<ref name="pmid2986972">{{cite 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 = 95–9 | year = 1985 | month = May | pmid = 2986972 | doi = 10.1111/j.1432-1033.1985.tb08898.x| url = | issn = }}</ref><ref name="pmid3004982">{{cite journal | author = Gabellini N, Sebald W | 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 = 569–79 | year = 1986 | month = February | pmid = 3004982 | doi = 10.1111/j.1432-1033.1986.tb09437.x| url = | issn = }}</ref>
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== 3D structure ==
== 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 [Fe<sub>2</sub>S<sub>2</sub>] cluster-binding subdomains have the topology of an incomplete antiparallel β-barrel. One iron atom of the Rieske [Fe<sub>2</sub>S<sub>2</sub>] cluster in the [[cytochrome b6f complex]] in the [[thylakoid]] membrane is coordinated by two [[cysteine]] residues and the other is coordinated by two [[histidine]] residues through the N<sup>δ</sup> atoms. The ligands coordinating the cluster originate from two loops; each loop contributes one Cys and one His.
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 variable numbers of α-helices. 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 [Fe<sub>2</sub>S<sub>2</sub>] cluster-binding subdomains have the topology of an incomplete antiparallel β-barrel. One iron atom of the Rieske [Fe<sub>2</sub>S<sub>2</sub>] cluster in the domain is coordinated by two [[cysteine]] residues and the other is coordinated by two [[histidine]] residues through the N<sup>δ</sup> atoms. The ligands coordinating the cluster originate from two loops; each loop contributes one Cys and one His.


== Subfamilies ==
== Subfamilies ==
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* {{cite journal | author=Schmidt, C.L. | title=Rieske iron-sulfur proteins from extremophilic organisms | journal=J. Bioenerg. Biomembr. | year=2004 | volume=36 | pages=107–113 | pmid=15168614 | doi=10.1023/B:JOBB.0000019602.96578.78 | issue=1}}
* {{cite journal | author=Schmidt, C.L. | title=Rieske iron-sulfur proteins from extremophilic organisms | journal=J. Bioenerg. Biomembr. | year=2004 | volume=36 | pages=107–113 | pmid=15168614 | doi=10.1023/B:JOBB.0000019602.96578.78 | issue=1}}
* {{cite journal | author=Schneider, D. and Schmidt, C.L. | title=Multiple Rieske proteins in prokaryotes: where and why? | journal=Biochim. Biophys. Acta | year=2005 | volume=1710 | pages=1–12 | pmid=16271700 | issue=1 | doi=10.1016/j.bbabio.2005.09.003}}
* {{cite journal | author=Schneider, D. and Schmidt, C.L. | title=Multiple Rieske proteins in prokaryotes: where and why? | journal=Biochim. Biophys. Acta | year=2005 | volume=1710 | pages=1–12 | pmid=16271700 | issue=1 | doi=10.1016/j.bbabio.2005.09.003}}
* {{cite journal | author=Brown, E.N. and Friemann, R. and Karlsson, A. and Parales, J.V. and Couture, M.M. and Eltis, L.D. and Ramaswamy, S. | title=Determining Rieske cluster reduction potentials | journal=J.Biol.Inorg.Chem. | year=2008 | volume=13 | pages=1301-1313 | pmid=18719951 | doi=10.1007/s00775-008-0413-4}}
{{refend}}
{{refend}}


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* {{PDB|1FQT}} - X-ray structure of Rieske-type ferredoxin associated with biphenyl dioxygenase from ''[[Burkholderia cepacia]]''
* {{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''
* {{PDB|1G8J}} - X-ray structure of Rieske subunit of arsenite oxidase from ''Alcaligenes faecalis''
* {{PDB|2I7F}} - X-ray structure of the ''Sphingomonas yanoikuyae B1'' Rieske ferredoxin
* {{PDB|2QPZ}} - X-ray structure of the [[Pseudomonas]] Naphthalene 1,2-dioxygenase Rieske ferredoxin
* {{InterPro|IPR005806}} - InterPro entry for Rieske [2Fe-2S] region
* {{InterPro|IPR005806}} - InterPro entry for Rieske [2Fe-2S] region


Revision as of 17:46, 7 November 2010

Mitochondrial cytochrome bc1 complex. (PDB: 1bcc​)
Identifiers
SymbolRieske
PfamPF00355
InterProIPR005806
PROSITEPDOC00177
SCOP21rie / SCOPe / SUPFAM
TCDB3.E.2
OPM protein1q90
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ww9A: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 3en1 3eqq 3dqy 2qpz 2gbw 2gbx

2i7f

Rieske proteins are iron-sulfur protein (ISP) components of cytochrome bc1 complexes and cytochrome b6f complexes which were first discovered and isolated by John S. Rieske and co-workers in 1964.[1]. It is a unique [2Fe-2S] cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria with widely ranging electron reduction potentials from -150 to +400 mV[2].

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.[3][4]

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.[5] 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.[6]

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.[3][6] 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.[7] 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
Rieske iron-sulfur center

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 variable numbers of α-helices. 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 in the domain 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

  1. ^ 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:10.1016/0006-291X(64)90171-8. {{cite journal}}: Cite has empty unknown parameter: |month= (help)CS1 maint: multiple names: authors list (link)
  2. ^ Brown, E.N. and Friemann, R. and Karlsson, A. and Parales, J.V. and Couture, M.M. and Eltis, L.D. and Ramaswamy, S. (2008). "Determining Rieske cluster reduction potentials". J.Biol.Inorg.Chem. 13: 1301–1313. doi:10.1007/s00775-008-0413-4. PMID 18719951.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ a b Harnisch U, Weiss H, Sebald W (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:10.1111/j.1432-1033.1985.tb08898.x. PMID 2986972. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ Gabellini N, Sebald W (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:10.1111/j.1432-1033.1986.tb09437.x. PMID 3004982. {{cite journal}}: Unknown parameter |month= ignored (help)
  5. ^ Kurowski B, Ludwig B (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. {{cite journal}}: Unknown parameter |month= ignored (help)
  6. ^ a b Madueño F, Napier JA, Cejudo FJ, Gray JC (1992). "Import and processing of the precursor of the Rieske FeS protein of tobacco chloroplasts". Plant Mol. Biol. 20 (2): 289–99. doi:10.1007/BF00014496. PMID 1391772. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  7. ^ Link TA (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:10.1016/S0014-5793(97)00772-2. PMID 9256231. {{cite journal}}: Unknown parameter |month= ignored (help)

Further reading

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
  • PDB: 2I7F​ - X-ray structure of the Sphingomonas yanoikuyae B1 Rieske ferredoxin
  • PDB: 2QPZ​ - X-ray structure of the Pseudomonas Naphthalene 1,2-dioxygenase Rieske ferredoxin
  • InterPro: IPR005806 - InterPro entry for Rieske [2Fe-2S] region
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