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Article
Promoting P450 BM3 heme domain dimerization with a tris(5-iodoacetamido-1,10-phenanthroline)Ru(II) complex
Biotechnology and Applied Biochemistry
  • Mallory Kato, San Jose State University
  • Bridget Foley, San Jose State University
  • Julia Vu, San Jose State University
  • Michael Huynh, San Jose State University
  • Kathreena Lucero, San Jose State University
  • Caroline Harmon, San Jose State University
  • Lionel Cheruzel, San Jose State University
Publication Date
7-1-2020
Document Type
Article
DOI
10.1002/bab.1970
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 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.

Funding Number
SC3GM095415
Funding Sponsor
National Institutes of Health
Keywords
  • dimerization,
  • gel electrophoresis,
  • iodoacetamido
Citation Information
Mallory Kato, Bridget Foley, Julia Vu, Michael Huynh, et al.. "Promoting P450 BM3 heme domain dimerization with a tris(5-iodoacetamido-1,10-phenanthroline)Ru(II) complex" Biotechnology and Applied Biochemistry Vol. 67 Iss. 4 (2020) p. 536 - 540
Available at: http://works.bepress.com/lionel-cheruzel/80/