The mechanism by which the cytochrome bc1 complex transfers electrons from ubiquinol to cytochrome c and links this electron transfer to proton translocation is the protonmotive Q cycle, shown above.
Our research is devoted to understanding the cytochrome bc1 complex, an essential respiratory enzyme. This site is intended to introduce you to the research projects in the Trumpower lab and the people who are working on those research projects. I hope you enjoy your "virtual visit," and that you will come visit us in person.
Bernard Trumpower
The bc1 complex is a structural dimer, as illustrated by the yeast enzyme below (Protein Data Bank code 1EZV). The redox subunits, cytochrome b (green), the Rieske iron-sulfur protein (blue), and cytochrome c1 (red) are colored in one monomer and shown as ribbons. Redox centers (c1, bL and bH hemes, and the FeS cluster), stigmatellin (Stg) and ubiquinone (Ubi) are shown as ball-and-stick models. Note the trans-membrane helix of the Rieske protein that is imbedded in one monomer and connects through a flexible linker region to the iron-sulfur cluster containing domain that interacts with the other monomer, and the overlapping N-termini of the cytochrome b subunits.
