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SRPBCC family protein
This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands. (from Pfam)
Rieske 2Fe-2S domain-containing protein
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. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilises the protein [4]. [1]. 8736555. 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.. Iwata S, Saynovits M, Link TA, Michel H. Structure 1996;4:567-579.. [2]. 1961737. Functional analysis in yeast of cDNA coding for the. mitochondrial Rieske iron-sulfur protein of higher plants.. Huang JT, Struck F, Matzinger DF, Levings CS;. Proc Natl Acad Sci U S A 1991;88:10716-10720.. [3]. 8386158. 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.. Brandt U, Yu L, Yu CA, Trumpower BL;. J Biol Chem 1993;268:8387-8390.. [4]. 19862563. Role of a novel disulfide bridge within the all-beta fold of. soluble Rieske proteins.. Botelho HM, Leal SS, Veith A, Prosinecki V, Bauer C, Frohlich R,. Kletzin A, Gomes CM;. J Biol Inorg Chem. 2010;15:271-281. (from Pfam)
anthranilate 1,2-dioxygenase large subunit AndAc
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