Structural highlights
Function
CYC_HORSE Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity).
Publication Abstract from PubMed
In the present study, the interactions between cisplatin and cytochrome c are investigated. Based on high-resolution X-ray diffraction data, two monometalated species, i.e. cyt c-Pt(NH3)2 and cyt c-Pt(NH3)2Cl, are found to be the main adducts that form in the reaction between the protein and the drug. Both monodentate and bidentate platinum coordination to the protein is observed, with platinum binding either to Met65 or to Met65 and Glu61, simultaneously.
The X-ray structure of the primary adducts formed in the reaction between cisplatin and cytochrome c.,Ferraro G, Messori L, Merlino A Chem Commun (Camb). 2015 Jan 29;51(13):2559-61. doi: 10.1039/c4cc09056j. PMID:25567806[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ferraro G, Messori L, Merlino A. The X-ray structure of the primary adducts formed in the reaction between cisplatin and cytochrome c. Chem Commun (Camb). 2015 Jan 29;51(13):2559-61. doi: 10.1039/c4cc09056j. PMID:25567806 doi:http://dx.doi.org/10.1039/c4cc09056j
