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A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc
2018
Metallomics
Preserved Fulltext
The NMR solution structure of a Pseudomonas metallothionein reveals a different binding capacity for ZnII and CdII ions that results in two novel metal-cluster topologies. Replacement of a non-coordinating residue by histidine decreases the kinetic lability of the cluster. All three structures reported show an identical protein fold.
doi:10.1039/c8mt00193f
pmid:30191219
fatcat:vu7hljyywrgwnod5bgbelndnpi