Silver binding to Pseudomonas aeruginosa azurin.
The interaction between azurin and silver ions was investigated, by means of ultraviolet, fluorescence and atomic absorption spectroscopies, as a function of the redox state of the protein. The Ag(I) ion has a very low affinity for oxidized azurin. Interestingly, the affinity is much higher for reduced azurin; in this case Ag(I) completely displaces the Cu(I) ion from the native binding site. The effect is very specific for silver ions since other ions, such as Hg(II), Ni(II) and Cd(II), do not produce the same effect. Treatment of reduced and oxidized azurin with excess Ag(I) (2-8-fold stoichiometric) shows that there is a second binding site for silver ions on the protein which can also bind Cu(II) and Hg(II) with comparable affinities.
Tordi
M G
MG
Dipaztimento di Scienze Biochimiche, CNR, Università di Roma, La Sapienza, Roma, Italia.
Naro
F
F
Giordano
R
R
Silvestrini
M C
MC
D001400:Azurin / Q000378:metabolism*; D001665:Binding Sites; D003300:Copper / Q000378:metabolism; D010084:Oxidation-Reduction; D011485:Protein Binding; D011550:Pseudomonas aeruginosa / Q000378:metabolism; D012834:Silver / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013054:Spectrophotometry, Atomic
D001400:Azurin; D012834:Silver; D003300:Copper