Salih B, Masselon C, Zenobi R
Department of Chemistry, ETH Zentrum, Zürich, Switzerland.
J Mass Spectrom. 1998 Oct;33(10):994-1002. doi: 10.1002/(SICI)1096-9888(1998100)33:10<994::AID-JMS714>3.0.CO;2-#.
Transition metal ion complexes with proteins and peptides are important in many areas of analytical and biological chemistry. We used positive and negative ion MALDI-MS to detect complexes with Cu and Ni ions, and show that the specific and non-specific transition metal ion-peptide complexes can be distinguished by the use of different analytical protocols. The pH dependent stability of these complexes is also reflected in the MALDI data. We further show that triple complexes of peptides or protein with chelated metal ions can be detected efficiently and rapidly by MALDI mass spectrometry. Such triple complexes play an important role in metal chelate affinity chromatography, where histidine containing biopolymers in particular are thought to bind metal-ligand complexes, depending on the oxidation state of the metal and the number of unoccupied coordination sites of the ligand.
过渡金属离子与蛋白质和肽的络合物在分析化学和生物化学的许多领域都很重要。我们使用正离子和负离子基质辅助激光解吸电离质谱（MALDI-MS）来检测与铜离子和镍离子的络合物，并表明通过使用不同的分析方法可以区分特异性和非特异性过渡金属离子-肽络合物。这些络合物的pH依赖性稳定性也反映在MALDI数据中。我们进一步表明，通过MALDI质谱可以高效、快速地检测肽或蛋白质与螯合金属离子的三元络合物。这种三元络合物在金属螯合亲和色谱中起着重要作用，在该色谱中，特别是含组氨酸的生物聚合物被认为会根据金属的氧化态和配体未占据配位位点的数量结合金属-配体络合物。
