ArticleJournal of inorganic biochemistry2012
Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ion.
Article in Journal of inorganic biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 12 citations in OpenAlex.
- Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site.Chembiochem : a European journal of chemical biology · 2018Article
- Bridging of a substrate between cyclodextrin and an enzyme's active site pocket triggers a unique mode of inhibition.Biochimica et biophysica acta · 2015Article
- A manganese-rich environment supports superoxide dismutase activity in a Lyme disease pathogen, Borrelia burgdorferi.The Journal of biological chemistry · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We report herein, for the first time, that Europium ion (Eu(3+)) binds to the "apo" form of Escherichia coli methionine aminopeptidase (EcMetAP), and such binding results in the activation of the enzyme as well as enhancement in the luminescence intensity of the metal ion. Due to competitive displacement of the enzyme-bound Eu(3+) by different metal ions, we could determine the binding affinities of both "activating" and "non-activating" metal ions for the enzyme via fluorescence spectroscopy. The experimental data revealed that among all metal ions, Fe(2+) exhibited the highest binding affinity for the enzyme, supporting the notion that it serves as the physiological metal ion for the enzyme. However, the enzyme-metal binding data did not adhere to the Irving-William series. On accounting for the binding affinity vis a vis the catalytic efficiency of the enzyme for different metal ions, it appears evident that that the "coordination states" and the relative softness" of metal ions are the major determinants in facilitating the EcMetAP catalyzed reaction.
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Registered trials
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