title: Destructive interactions of dirhodium(II) tetraacetate with β metallothionein rh1a.
abstract: Metal-based therapeutics are vital tools in medicine. Metal-chelating proteins can dramatically decrease drug efficacy. Dirhodium(II) tetraacetate, a potential anticancer compound, binds in vitro to 8 cysteines of the human metallothionein 1a β-fragment. Electrospray ionization mass spectrometry shows that the final product is the Rh2(4+) core encapsulated by the β fragment of the metallothionein protein protein.
authors.affiliation: Department of Chemistry, The University of Western Ontario, London, ON N6A 5B7, Canada. stillman@uwo.ca.
authors.forename: Daisy L
authors.initials: DL
authors.lastname: Wong
authors.affiliation: Department of Chemistry, The University of Western Ontario, London, ON N6A 5B7, Canada. stillman@uwo.ca.
authors.forename: Martin J
authors.initials: MJ
authors.lastname: Stillman