Abstract
Metalloproteins play an important role in many biochemical processes such as respiration, metabolism, photosynthesis, nitrogen fixation, nerve transmission, muscle contraction, and signal transduction. Determining the details of the structure of the metal-center is central to understanding the structure and function of a metalloprotein, as the metal-center is usually the site of catalytic activity. For structure-function studies, metalloproteins are often produced by overexpression of recombinant genes. Frequently, a recombinant metalloprotein is produced in a denatured form, with its metal center absent. In such cases the protein must be activated by inserting the metal atoms and allowing the protein to fold into its native structure. There is a need for a rapid, accurate assay of these recombinant metalloproteins to determine the subunit amino acid composition, the metal stoichiometry, and the subunit stoichiometry. We have been investigating the capability of mass spectrometry to make such measurements for multimeric metalloproteins.
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Kulkarni, S.S., Taylor, P.K., Kurtz, D.M., Amster, I.J. (1998). Electrospray Ionization FTICR Spectrometry of Metalloproteins. In: Ens, W., Standing, K.G., Chernushevich, I.V. (eds) New Methods for the Study of Biomolecular Complexes. NATO ASI Series, vol 510. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9046-4_12
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DOI: https://doi.org/10.1007/978-94-015-9046-4_12
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