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10544253980
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note
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-1 for apoproteins.
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45
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10544220167
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note
-
The ES-MS data were acquired in the continuum mode using a Quattro mass spectrometer capable of unit mass resolution to 4000 molecular weight (50% valley definition). The mass scale was calibrated with CsI. The electrospray ionization was performed with a 100% water flow system at 15 μL/min into the ion source, and the sample was in ammonium acetate (pH 5.1) buffer. Multiple charged ions (typically 6, 7, and 8 positive-charged species) were observed under the conditions employed. The multiple charged data were then transformed into the singly charged spectra presented in the paper. (22) In this paper, we use MM' to represent different metal derivatives in this binuclear copper center, where M is in the putative Cu(II) site, M' is in the putative Cu(I) site, and an E represents an empty site.
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-
-
-
46
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10544242682
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note
-
The absorption bands are similar to those observed in the Hg(II) titration into the holoprotein (Figure 1Ab), but the peaks are less well-defined as revealed by difference spectra (data not shown).
-
-
-
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47
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10544242081
-
-
note
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2+. Therefore, the metal affinity for the putative Cu(II) site is in the order of Hg(II) > 2Ag(I) > Cu(II) and the metal affinity for the putative Cu(I) site is Ag(I) > Cu(I) > Hg(II).
-
-
-
-
48
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10544221365
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note
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An alternative explanation can rationalize the observation that Hg-(II) replaces Cu(II) preferentially and Hg(II)Ag(I) is the most stable derivative; the purple copper center is built so that a net +4-charged M(II)M(II) in the binding site is less favored than the +3-charged M(II)M(I) derivative.
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