Bacterial sensors define intracellular free energies for correct enzyme metalation
| Autor: | Maria Alessandra Martini, Nigel J. Robinson, Martin J. Warren, Peter T. Chivers, Andrew J. P. Scott, Thomas G. Huggins, Deenah Osman, Evelyne Deery, Richard Morton, Elena Lurie-Luke, Andrew W. Foster, Jonathan W. Steed, Junjun Chen, Andy Lawrence |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Metalation
Allosteric regulation chemistry.chemical_element Bacterial Physiological Phenomena Article Metal 03 medical and health sciences symbols.namesake Bacterial Proteins Salmonella Metalloproteins Metalloprotein Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Bacteria Chemistry 030302 biochemistry & molecular biology Affinity Labels Cell Biology C700 Affinities Combinatorial chemistry Gibbs free energy Energy Transfer Metals visual_art visual_art.visual_art_medium symbols Cobalt Intracellular |
| Zdroj: | Nature chemical biology Nature chemical biology, 2019, Vol.15(3), pp.241-249 [Peer Reviewed Journal] |
| ISSN: | 1552-4450 |
| Popis: | There is a challenge for metalloenzymes to acquire their correct metals because some inorganic elements form more stable complexes with proteins than do others. These preferences can be overcome provided some metals are more available than others. However, while the total amount of cellular metal can be readily measured, the available levels of each metal have been more difficult to define. Metal-sensing transcriptional regulators are tuned to the intracellular availabilities of their cognate ions. Here we have determined the standard free energy for metal complex formation to which each sensor, in a set of bacterial metal sensors, is attuned: the less competitive the metal, the less favorable the free energy and hence the greater availability to which the cognate allosteric mechanism is tuned. Comparing these free energies with values derived from the metal affinities of a metalloprotein reveals the mechanism of correct metalation exemplified here by a cobalt chelatase for vitamin B 12 . |
| Databáze: | OpenAIRE |
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