Promoting P450 BM3 heme domain dimerization with a tris(5-iodoacetamido-1,10-phenanthroline)Ru(II) complex
Biotechnology and Applied Biochemistry
Protein dimerization often occurs in many biological systems as to provide structural and functional advantages. A tris(5-iodoacetamido-1,10-phenanthroline)Ruthenium(II) complex was shown to promote the covalent dimerization of a P450 BM3 heme domain mutant containing a surface-exposed nonnative single cysteine residue. The formation of homodimeric species was confirmed by protein gel electrophoresis, mass spectrometry and UV–Vis spectroscopy. The dimeric species could be separated from the monomer and aggregates by size-exclusion chromatography. Docking simulation reveals a plausible structure with two proteins covalently conjugated to the inorganic compound.
National Institutes of Health
dimerization, gel electrophoresis, iodoacetamido
Mallory Kato, Bridget Foley, Julia Vu, Michael Huynh, Kathreena Lucero, Caroline Harmon, and Lionel Cheruzel. "Promoting P450 BM3 heme domain dimerization with a tris(5-iodoacetamido-1,10-phenanthroline)Ru(II) complex" Biotechnology and Applied Biochemistry (2020): 536-540. https://doi.org/10.1002/bab.1970