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Rieske protein

From Wikipedia, the free encyclopedia

Rieske iron-sulfur center
Rieske iron-sulfur center

The iron-sulfur protein (ISP) component of cytochrome bc1 complex was first discovered and isolated by John S. Rieske and co-workers in 1964. 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

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.

[edit] References

  • 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. PMID 16168954. 
  • Link, T.A. (1997). "The role of the 'Rieske' iron sulfur protein in the hydroquinone oxidation (QP) site of the cytochrome bc1 complex. The 'proton-gated affinity change' mechanism". FEBS Lett. 412: 257–264. PMID 9256231. 
  • Mason, J.R. and Cammack, R. (1992). "The electron-transport proteins of hydroxylating bacterial dioxygenases". Annu. Rev. Microbiol. 46: 277–305. PMID 1444257. 
  • Rieske, J.S., Maclennan, D.H. and 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. 
  • Schmidt, C.L. (2004). "Rieske iron-sulfur proteins from extremophilic organisms". J. Bioenerg. Biomembr. 36: 107–113. 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. 

[edit] 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
  • InterPro IPR005806 - InterPro entry for Rieske [2Fe-2S] region
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