Cytochrome C1
| Cytochrom_C1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 native structure of bovine mitochondrial cytochrome bc1 complex | |||||||||
| Identifiers | |||||||||
| Symbol | Cytochrom_C1 | ||||||||
| Pfam | PF02167 | ||||||||
| Pfam clan | CL0318 | ||||||||
| InterPro | IPR002326 | ||||||||
| SCOP | 3bcc | ||||||||
| SUPERFAMILY | 3bcc | ||||||||
| TCDB | 3.D.3 | ||||||||
| |||||||||
Cytochrome C1 is formed in the cytosol and targeted to the mitochondrial intermembrane space. It is one of the constituents of complex III, which forms the third proton pump in the mitochondrial electron transport chain.
Cytochrome c1 is a subunit of the electron transport chain protein Ubiquinol Cytochrome c Reductase (UQCR, Complex III or Cytochrome bc1 complex), which consists of the products of one mitochondrially encoded gene, MTCYTB (mitochondrial cytochrome b) and ten nuclear genes: UQCRC1, UQCRC2, Cytochrome c1, UQCRFS1 (Rieske protein), UQCRB, UQCRQ[1] ("11kDa protein"), UQCRH (cyt c1 Hinge protein), Rieske Protein presequence, "cyt. c1 associated protein", and UQCR[2] ("Rieske-associated protein").
Ubiquinol:ferricytochrome c oxidoreductase is found in mitochondria, photosynthetic bacteria and other prokaryotes. The general function of the complex is electron transfer between two mobile redox carriers, ubiquinol and cytochrome c; the electron transfer is coupled with proton translocation across the membrane, thus generating proton-motive force in the form of an electrochemical potential difference that can drive ATP synthesis. In its structure and functions, the cytochrome bc1 complex bears extensive analogy to the cytochrome b6f complex of chloroplasts and cyanobacteria; cyt c1 plays an analogous role to cytochrome f, in spite of their different structures.[3]
External links
- Cytochrome c1 at the US National Library of Medicine Medical Subject Headings (MeSH)
References
- ↑ http://www.ncbi.nlm.nih.gov/nuccore/98986462[]
- ↑ http://www.ncbi.nlm.nih.gov/nucleotide/19923785[]
- ↑ Prince, Roger C.; George, Graham N. (1995). "Cytochrome f revealed". Trends in Biochemical Sciences 20 (6): 217–8. doi:10.1016/S0968-0004(00)89018-0. PMID 7631417.
This article incorporates text from the public domain Pfam and InterPro IPR002326