ring-hydroxylating dioxygenase, large terminal subunit [Mycolicibacter - Protein

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Role of a novel disulfide bridge within the all-beta fold of soluble Rieske proteins. [J Biol Inorg Chem. 2010]
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, Fröhlich R, Kletzin A, Gomes CM. J Biol Inorg Chem. 2010 Feb; 15(2):271-81. Epub 2009 Oct 28.
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. [Structure. 1996]
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 May 15; 4(5):567-79.
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. [J Biol Chem. 1993]
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 Apr 25; 268(12):8387-90.

RefSeq protein
See the reference protein sequence for MULTISPECIES: Rieske 2Fe-2S domain-containing protein (WP_036388754.1).

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ring-hydroxylating dioxygenase, large terminal subunit [Mycolicibacterium concep...
ring-hydroxylating dioxygenase, large terminal subunit [Mycolicibacterium conceptionense]
gi|808669982|emb|CQD05103.1||gnl|WG F|CQD05103

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