Almost half of all enzymes must associate with a particular metal to function. An ambition is
to understand why each metal–protein partnership arose and how it is maintained. Metal …

Selective metal coordination is central to the functions of metalloproteins:, each
metalloprotein must pair with its cognate metallocofactor to fulfil its biological role. However …

The metal binding preferences of most metalloproteins do not match their metal
requirements. Thus, metallation of an estimated 30% of metalloenzymes is aided by metal …

Metalloproteins play structural and catalytic roles in gene expression. The metalloregulatory
proteins are a subclass that exerts metal-responsive control of genes involved in respiration …

Metalloregulatory proteins control the expression of genes that allow organisms to quickly
adapt to chronic toxicity or deprivation of both biologically essential metal ions and heavy …

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 …

Intracellular zinc is thought to be available in a cytosolic pool of free or loosely bound Zn (II)
ions in the micromolar to picomolar range. To test this, we determined the mechanism of zinc …

Protein metal-coordination sites are richly varied and exquisitely attuned to their inorganic
partners, yet many metalloproteins still select the wrong metals when presented with …

Copper is an essential trace element for eukaryotes and most prokaryotes. However,
intracellular free copper must be strictly limited because of its toxic side effects. Complex …

The essential transition metal ions are avidly accumulated by cells, yet they have two faces:
They are put to use as required cofactors, but they also can catalyze cytotoxic reactions …