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Palladium(II) and platinum(II) bind strongly to an engineered blue copper protein.

ABSTRACT: Studies of palladium(II) and platinum(II) binding to well-characterized proteins contribute to understanding the influence of these metals in the environment and body. The well-characterized apoprotein of azurin has a soft-metal binding site that may be exposed to solvent by mutation of a coordinating His-117 residue to glycine (H117G). Palladium(II) and platinum(II) form strong 1:1 adducts with the apo form of H117G azurin. A combination of UV-vis, circular dichroism, and inductively coupled plasma mass spectrometry techniques suggests that the metal binds specifically at His-46 and Cys-112 of the protein.

SUBMITTER: McLaughlin MP

PROVIDER: S-EPMC3217333 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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Palladium(II) and platinum(II) bind strongly to an engineered blue copper protein.

McLaughlin Matthew P MP Darrah Thomas H TH Holland Patrick L PL

Inorganic chemistry 20111025 22

Studies of palladium(II) and platinum(II) binding to well-characterized proteins contribute to understanding the influence of these metals in the environment and body. The well-characterized apoprotein of azurin has a soft-metal binding site that may be exposed to solvent by mutation of a coordinating His-117 residue to glycine (H117G). Palladium(II) and platinum(II) form strong 1:1 adducts with the apo form of H117G azurin. A combination of UV-vis, circular dichroism, and inductively coupled pl ...[more]

PMID: 22026434

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