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

Authors

Mallory Kato, San Jose State UniversityFollow
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 UniversityFollow

Publication Date

7-1-2020

Document Type

Article

Publication Title

Biotechnology and Applied Biochemistry

Volume

67

Issue

4

DOI

10.1002/bab.1970

First Page

536

Last Page

540

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

Department

Chemistry

Recommended Citation

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