Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.5.1 extracted from

  • Iverson, T.M.; Luna-Chavez, C.; Croal, L.R.; Cecchini, G.; Rees, D.C.
    Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site (2002), J. Biol. Chem., 277, 16124-16130.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of QFR to 3.3 A resolution. Enzyme contains two quinone species, presumably menaquinol, bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed QP and QD, indicating their positions proximal, QP, or distal, QD, to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. Co-crystallization studies of the Escherichia coli QFR with the quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH2 at the QP site. In the structures with the inhibitor bound at QP, no density is observed at QD. The conserved acidic residue, Glu29 in subunit FrdC, in the Escherichia coli enzyme may act as a proton shuttle from the quinol during enzyme turnover Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-heptyl-4-hydroxyquinoline N-oxide inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies Escherichia coli
2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P00363
-
-

Synonyms

Synonyms Comment Organism
QFR
-
Escherichia coli