Rieske protein

From Wikipedia, the free encyclopedia

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 N^δ 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 (Q_P) 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