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. Show the loops containing the ligands. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q 0 site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed: 1657998 , PubMed: 2538628 ) (Probable). This “virtual” Rieske structure was subsequently reintegrated into the parent enzymes cyt bc 1, cyt b 6 f complex, and arsenite oxidase by structure alignment of the β-sheet skeleton with that of the genuine Rieske protein present in the complex and subsequently deleting the latter from the structure file. Protein abundance of Rieske FeS and Cytochrome f subunits of cytb 6 f was analysed on leaf area basis in the T … 2 Publications Highlight groups of interest Show ligands to the 2Fe2S center. The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc1 functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544). The structure shows an overall fold similar to previously reported Rieske proteins. Show the loops containing the ligands.

The spectroscopic and electrochemical properties of the ‘Rieske’ [2Fe–2S] cluster differ significantly from those of other iron–sulfur clusters. Rieske FeS overexpression increases Cytochrome b 6 f content. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. Abstract. The Rieske iron-sulfur protein, one of the catalytic subunits of the cytochrome complex, is involved in electron transfer at the level of the inner membrane of yeast mitochondria. Unlike other Rieske aromatic oxygenases, DMO oxygenates the exocyclic methyl group, rather than the aromatic ring, of its substrate. Rieske's Iron Sulfur Protein 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 Å resolution. The Rieske iron-sulfur protein is encoded by nuclear DNA and, after being synthesized in the cytosol, is imported into mitochondria with the help of a cleavable N-terminal presequence.

Rieske's Iron Sulfur Protein 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 Å resolution. The Rieske 2Fe-2S protein is a central component of the photosynthetic electron transport cytochrome b6f complex in chloroplast and cyanobacterial thylakoid membranes.

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