Here we report on the reaction of rhenate anions (ReO(3) (-)) with multiply protonated peptide cations in a quadrupole linear ion trap mass spectrometer. These reactions effect the formation of an anion-cation complex that, upon collisional activation, dissociates along the peptide backbone rather than by displacement of the anion. Cleavage of the peptide backbone, with anion retention, leads us to conclude the anion-cationcomplexmust be tightly bound, most probably through coordination chemistry. We describe this chemistry and detail the possible application of such ion attachment reactions to the characterization of intact proteins.

中文翻译：

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在真空中形成肽-金属配位配合物

在这里，我们报告了四极杆线性离子阱质谱仪中铼酸阴离子 (ReO(3) (-)) 与多质子化肽阳离子的反应。这些反应影响阴离子-阳离子复合物的形成，该复合物在碰撞活化时沿着肽主链解离，而不是通过取代阴离子。肽主链的裂解，阴离子保留，使我们得出结论，阴离子-阳离子复合物必须紧密结合，最有可能通过配位化学。我们描述了这种化学并详细说明了这种离子附着反应在完整蛋白质表征中的可能应用。