Structural highlights
Function
CYC1_YEAST 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.
Publication Abstract from PubMed
The interactions of two mono-functionalized sulfonatocalix[4]arenes with cytochrome c were investigated by structural and thermodynamic methods. The replacement of a single sulfonate with either a bromo or a phenyl substituent resulted in altered recognition of cytochrome c as evidenced by X-ray crystallography. The bromo-substituted ligand yielded a new binding mode in which a self-encapsulated calixarene dimer contributed to crystal packing. This ligand also formed a weak halogen bond with the protein. The phenyl-substituted ligand was bound to Lys4 of cytochrome c, in a 1.7 A resolution crystal structure. A dimeric packing arrangement mediated by ligand-ligand contacts in the crystal suggested a possible assembly mechanism. The different protein recognition properties of these calixarenes are discussed.
Protein Recognition by Functionalized Sulfonatocalix[4]arenes.,Doolan AM, Rennie ML, Crowley PB Chemistry. 2018 Jan 19;24(4):984-991. doi: 10.1002/chem.201704931. Epub 2017 Dec , 13. PMID:29125201[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doolan AM, Rennie ML, Crowley PB. Protein Recognition by Functionalized Sulfonatocalix[4]arenes. Chemistry. 2018 Jan 19;24(4):984-991. doi: 10.1002/chem.201704931. Epub 2017 Dec , 13. PMID:29125201 doi:http://dx.doi.org/10.1002/chem.201704931
