期刊
METALLOMICS
卷 8, 期 6, 页码 605-617出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5mt00209e
关键词
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资金
- NSF [CHE-1151957, CHE-1308598]
- Institutional Development Award from NIGMS [P20GM0103423]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1555839, 1308598] Funding Source: National Science Foundation
Isothermal titration calorimetry (ITC) was used to quantify the thermodynamics of Pb2+ and Zn2+ binding to metallothionein-3 (MT-3). Pb2+ binds to zinc-replete Zn7MT-3 displacing each zinc ion with a similar change in free energy (Delta G) and enthalpy (Delta H). EDTA chelation measurements of Zn7MT-3 and Pb7MT-3 reveal that both metal ions are extracted in a tri-phasic process, indicating that they bind to the protein in three populations with different binding thermodynamics. Metal binding is entropically favoured, with an enthalpic penalty that reflects the enthalpic cost of cysteine deprotonation accompanying thiolate ligation of the metal ions. These data indicate that Pb2+ binding to both apo MT-3 and Zn7MT-3 is thermodynamically favourable, and implicate MT-3 in neuronal lead biochemistry.
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