The ability of peptides to coordinate with specific metal ions is crucial for environmental protection and recycling processes, because of the toxicity and scarcity of the ions. One-third of proteins in biological systems have binding affinities to specific metal ions, and thus, can be further applied to collect precious metal ions. Zinc ion is a necessary co-factor for the regulation of physiological responses in biological systems, because of its ability to bind biomolecules. In this study, three zinc finger (ZF) domains (PARIS_ZF2-4) from Parkin-interacting substrates (PARIS) were used to harvest heterometals such as Co 2+ , Cu 2+ , and Fe 3+ in Escherichia coli. Spectroscopic results demonstrated that PARIS_ZF2-4 can coordinate with Co 2+ during expression. Purified PARIS_ZF2-4 generated specific d-d transition bands (570 and 644 nm), which were monitored upon the addition of Co 2+ to apo-PARIS_ZF2-4. These results can facilitate the possible applications of the ZF domain in heterometal substitution and elimination in biological systems.