期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 23, 期 5, 页码 785-793出版社
SPRINGER
DOI: 10.1007/s00775-018-1574-4
关键词
Metal binding; Manganese(II); Cobalt(II); Irving-Williams series; Isothermal titration calorimetry; Thermodynamics
资金
- National Institutes of Health [GM063584]
Taurine/alpha-ketoglutarate (alpha KG) dioxygenase (TauD) is an E. coli nonheme Fe2+- and alpha KG-dependent metalloenzyme that catalyzes the hydroxylation of taurine, leading to the production of sulfite. The metal-dependent active site in TauD is formed by two histidine and one aspartate that coordinating to one face of an octahedral coordination geometry, known as the 2-His-1-carboxylate facial triad. This motif is found in many nonheme Fe2+ proteins, but there is limited information on the thermodynamic parameters that govern metal-ion binding to this site. Here, we report data from calorimetry and related biophysical techniques to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to TauD, and these values are compared to the Fe2+ data reported earlier Henderson et al. (Inorg Chem 54: 2278-2283, 2015). The buffer-independent binding constants (K) were measured to be 1.6 x 10(6), 2.4 x 10(7), and 1.7 x 10(9), for Mn2+, Fe2+, and Co2+, respectively. The corresponding Delta GA degrees values were calculated to be - 8.4, - 10.1, and - 12.5 kcal/mol, respectively. The metal-binding enthalpy changes (Delta H) for these binding events are - 11.1 (+/- 0.1), - 12.2 (+/- 0.1), and - 16.0 (+/- 0.6) kcal/mol, respectively. These data are fully consistent with the Irving-Williams series, which show an increasing affinity for transition metal ions across the periodic table. It appears that the periodic increase in affinity, however, is a result of a complicated summation of enthalpy terms (including favorable metal-ion coordination processes and unfavorable ionization events) and related entropy terms.
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