Abstract
In the present work, traveling wave ion mobility spectrometry-mass spectrometry (TWIMS-MS) was applied to speciation analysis of metalloproteins. The influence of pH on complexation conditions between some metals and bovine carbonic anhydrase was evaluated from pH 6 to 9, as well as the time involved in their complexation (0–24 h). Employing TWIMS-MS, two conformational states of bovine carbonic anhydrase were observed with charge states of +12 and +11; these configurations being evaluated in terms of the folded state of the apo form and this protein (at charge state +11) being linked to barium, lead, copper, and zinc in their divalent forms. Metalloprotein speciation analysis was carried out for copper (Cu+ and Cu2+), lead (Pb2+ and Pb4+), and selenium (Se4+ and Se6+) species complexed with bovine carbonic anhydrase. Mobilities of all complexed species were compared, also considering the apo form of this protein.
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Acknowledgments
The authors thank the Fundação de Amparo a Pesquisa do Estado de São Paulo (São Paulo, Brazil) and the Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasília, Brazil) for financial support and fellowships. We are also grateful to Prof. Carol H. Collins for language assistance and Alexandre Ferreira Gomes for helping the authors with some experiments.
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Published in the topical collection (Bio)Analytical Research in Latin America with guest editors Marco A. Zezzi Arruda and Lauro Kubota.
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Pessôa, G.S., Pilau, E.J., Gozzo, F.C. et al. Ion mobility spectrometry focusing on speciation analysis of metals/metalloids bound to carbonic anhydrase. Anal Bioanal Chem 405, 7653–7660 (2013). https://doi.org/10.1007/s00216-013-7064-1
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DOI: https://doi.org/10.1007/s00216-013-7064-1