3H1K

Chicken cytochrome BC1 complex with ZN++ and an iodinated derivative of kresoxim-methyl bound

Summary for 3H1K

• Entry DOI: 10.2210/pdb3h1k/pdb
• Related: 1bbc 2fyu 2ppj 3cx5
• Descriptor: MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I, MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine, ... (22 entities in total)
• Functional Keywords: cytochrome bc1, membrane protein, heme protein, rieske iron sulfur protein, cytochrome b, cytochrome c1, complex iii, ubiquinone, oxidoreductase, redox enzyme, zinc, kresoxim-methyl, respiratory chain, electron transport, heme, inner membrane iron, membrane, metal-binding, mitochondrion, transmembrane, iron, mitochondrion inner membrane, transport, disulfide bond, iron-sulfur, transit peptide
• Biological source: Gallus gallus (chicken); More
• Total number of polymer chains: 20
• Total formula weight: 480849.89

Authors

Berry, E.A.,Zhang, Z.,Bellamy, H.D.,Huang, L.S. (deposition date: 2009-04-12, release date: 2009-04-28, Last modification date: 2023-09-06)

Primary citation

Berry, E.A.,Zhang, Z.,Bellamy, H.D.,Huang, L.
Crystallographic location of two Zn(2+)-binding sites in the avian cytochrome bc(1) complex
Biochim.Biophys.Acta, 1459:440-448, 2000

PubMed Abstract: The chicken mitochondrial ubiquinol cytochrome c oxidoreductase (bc(1) complex) is inhibited by Zn(2+) ions, but with higher K(i) ( approximately 3 microM) than the corresponding bovine enzyme. When equilibrated with mother liquor containing 200 microM ZnCl(2) for 7 days, the crystalline chicken bc(1) complex specifically binds Zn(2+) at 4 sites representing two sites on each monomer in the dimer. These two sites are close to the stigmatellin-binding site, taken to be center Q(o) of the Q-cycle mechanism, and are candidates for the inhibitory site. One binding site is actually in the hydrophobic channel between the Q(o) site and the bulk lipid phase, and may interfere with quinone binding. The other is in a hydrophilic area between cytochromes b and c(1), and might interfere with the egress of protons from the Q(o) site to the intermembrane aqueous medium. No zinc was bound near the putative proteolytic active site of subunits 1 and 2 (homologous to mitochondrial processing peptidase) under these conditions.

PubMed: 11004461

Experimental method

X-RAY DIFFRACTION (3.48 Å)