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Promoting P450 BM3 heme domain dimerization with a tris(5-iodoacetamido-1,10-phenanthroline)Ru(II) complex.

ABSTRACT: 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 non-native 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.

SUBMITTER: Kato M 

PROVIDER: S-EPMC7769117 | biostudies-literature | 2020 Jul-Aug

REPOSITORIES: biostudies-literature

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Promoting P450 BM3 heme domain dimerization with a tris(5-iodoacetamido-1,10-phenanthroline)Ru(II) complex.

Kato Mallory M   Foley Bridget B   Vu Julia J   Huynh Michael M   Lucero Kathreena K   Harmon Caroline C   Cheruzel Lionel L  

Biotechnology and applied biochemistry 20200617 4

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 non-native 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 mon  ...[more]

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