Recombinant Theropithecus gelada Cytochrome b-c1 complex subunit Rieske, mitochondrial (UQCRFS1)
Description
Protein Overview
UQCRFS1 is a nuclear-encoded subunit of mitochondrial Complex III (cytochrome bc₁ complex), essential for oxidative phosphorylation. The recombinant version is expressed in E. coli with a His-tag for purification and experimental tracking . Key attributes include:
Functional Role in Mitochondrial Respiration
UQCRFS1 is a catalytic core subunit of Complex III, enabling electron transfer from ubiquinol to cytochrome c₁ via a redox-driven Q-cycle mechanism . Key functions:
-
Electron Transport: Mediates transfer between ubiquinol (Q-pool) and cytochrome c₁, coupled with proton translocation .
-
Complex III Assembly: Incorporation of UQCRFS1 is the penultimate step in Complex III maturation, requiring chaperones like BCS1L and MZM1L .
Biochemical Interactions:
| Function | Associated Proteins/Complexes |
|---|---|
| 2Fe-2S cluster binding | MZM1L (LYRM7), BCS1L (assembly chaperones) |
| Ubiquinol oxidation | Cytochrome b (MT-CYB), Cytochrome c₁ (CYC1) |
Research Applications
This recombinant protein is widely used in:
-
Enzyme Kinetics: Studying electron transfer mechanisms and proton pumping in isolated Complex III .
-
Structural Biology: Crystallography and cryo-EM to resolve conformational states during catalysis .
-
Disease Models: Investigating mitochondrial disorders linked to Complex III dysfunction (e.g., mutations in BCS1L or TTC19) .
Product Specs
Note: While we prioritize shipping the format currently in stock, please specify any format requirements in your order notes for customized preparation.
Note: All proteins are shipped with standard blue ice packs. Dry ice shipping requires advance notice and incurs additional charges.
The tag type is determined during production. If you require a specific tag, please inform us, and we will prioritize its development.
Target Background
Recombinant Theropithecus gelada Cytochrome b-c1 complex subunit Rieske, mitochondrial (UQCRFS1) is a component of ubiquinol-cytochrome c oxidoreductase (Complex III), a multi-subunit transmembrane complex within the mitochondrial electron transport chain (ETC). The ETC drives oxidative phosphorylation, a crucial process for ATP synthesis. Complex III, along with succinate dehydrogenase (Complex II) and cytochrome c oxidase (Complex IV), facilitates electron transfer from NADH and succinate to molecular oxygen. This process generates an electrochemical gradient across the inner mitochondrial membrane, powering transmembrane transport and ATP synthase activity.
Complex III catalyzes electron transfer from ubiquinol to cytochrome c, coupling this redox reaction to proton translocation across the inner mitochondrial membrane via the Q cycle. This cycle consumes two protons from the matrix, releases four protons into the intermembrane space, and transfers two electrons to cytochrome c. The Rieske protein, a catalytic core subunit of Complex III, contains an iron-sulfur cluster essential for this electron transfer. UQCRFS1 undergoes post-translational processing upon incorporation into the Complex III dimer, yielding a fragment known as subunit 9 (corresponding to its mitochondrial targeting sequence, MTS). This processing is crucial for proper insertion into the complex. However, the persistence of UQCRFS1-derived fragments can hinder the processing and assembly of newly imported UQCRFS1, negatively impacting Complex III structure and function.
