Palladium(II) and platinum(II) bind strongly to an engineered blue copper protein.
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.
Department of Chemistry, University of Rochester, Rochester, New York 14618, United States.
Matthew P
MP
McLaughlin
Thomas H
TH
Darrah
Patrick L
PL
Holland
D001059:Apoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001400:Azurin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D010165:Palladium / Q000378:metabolism*; D010984:Platinum / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D015202:Protein Engineering; D011550:Pseudomonas aeruginosa / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001059:Apoproteins; D001426:Bacterial Proteins; D001400:Azurin; D010984:Platinum; D010165:Palladium; D003300:Copper