D. Xia et al., A novel electron transfer mechanism suggested by crystallographic studies of mitochondrial cytochrome bc1 complex, BIOC CELL B, 76(5), 1998, pp. 673-679
Citations number
27
Categorie Soggetti
Cell & Developmental Biology
Journal title
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE
The crystal structure of bovine mitochondrial cytochrome bc1 complex, an in
tegral membrane protein complex of 11 different subunits with a total molec
ular mass of 242 kDa, demonstrated a tightly associated dimer consisting of
three major regions: a matrix region primarily made of subunits core1, cor
e2, 6, and 9; a transmembrane-helix region of 26 helices in the dimer contr
ibuted by cytochrome b, cytochrome c1, the Rieske iron-sulfur protein (ISP)
, subunits 7, 10, and 11; and an intermembrane-space region composed of ext
ramembrane domains of ISP, cytochrome c1, and subunit 8. The structure also
revealed the positions of and distances between irons of prosthetic groups
, and two symmetry related cavities in the transmembrane-helix region upon
dimerization of the bc1 complex. Extensive crystallographic studies on crys
tals of bc1 complexed with inhibitors of electron transfer identified bindi
ng pockets for both Q(o) and Q(i) site inhibitors. Discrete binding sites f
or subtypes of Q(o) site inhibitors have been mapped onto the Q(o) binding
pocket, and bindings of different subtypes of Q(o) site inhibitors are capa
ble of inducing dramatic conformational changes in the extramembrane domain
of ISP. A novel electron transfer mechanism for the bc1 complex consistent
with crystallographic observations is discussed.