1RIE

STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX

Summary for 1RIE

Entry DOI	10.2210/pdb1rie/pdb
Descriptor	RIESKE IRON-SULFUR PROTEIN, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
Functional Keywords	oxidoreductase, cytochrome bc1 complex, histidine ligands, rieske iron-sulfur cluster, electron transport
Biological source	Bos taurus (cattle)
Cellular location	Mitochondrion inner membrane: P13272
Total number of polymer chains	1
Total formula weight	14616.48
Authors	Iwata, S.,Saynovits, M.,Link, T.A.,Michel, H. (deposition date: 1996-02-23, release date: 1996-12-07, Last modification date: 2024-10-23)
Primary citation	Iwata, S.,Saynovits, M.,Link, T.A.,Michel, H. 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, 4:567-579, 1996 Cited by PubMed Abstract: The 'Rieske' iron-sulfur protein is the primary electron acceptor during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly from those of other iron-sulfur clusters. A 129-residue water soluble fragment containing the intact [2Fe-2S] cluster was isolated following proteolytic digestion of the bc1 complex and used for structural studies. PubMed: 8736555 DOI: 10.1016/S0969-2126(96)00062-7 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation