Numerous biomolecules exhibit the ability to dissolve certain metal cations. Thus, proteins, polysaccharides, and polynucleic acids are excellent polydentate ligands for many metal ions.  Organic compounds such as the amino acids glutamic acid and histidine, organic diacids such as malate, and polypeptides such as phytochelatin are also typical chelators. In addition to these adventitious chelators, several biomolecules are specifically produced to bind certain metals (see next section).
Virtually all metalloenzymes feature metals that are chelated, usually to peptides or cofactors and prosthetic groups.  Such chelating agents include the porphyrin rings in hemoglobin and chlorophyll.  Many microbial species produce water-soluble pigments that serve as chelating agents, termed siderophores. For example,  species of Pseudomonas are known to secrete pyochelin and pyoverdine that bind iron. Enterobactin, produced by E. coli, is the strongest chelating agent known. The marine mussels use metal chelation esp. Fe chelation with the Dopa residues in mussel foot protein-1 to improve the strength of the threads that they use to secure themselves to surfaces.
In earth science, chemical weathering is attributed to organic chelating agents (e.g., peptides and sugars) that extract metal ions from minerals and rocks.  Most metal complexes in the environment and in nature are bound in some form of chelate ring (e.g., with a humic acid or a protein). Thus, metal chelates are relevant to the mobilization of metals in the soil, the uptake and the accumulation of metals into plants and microorganisms. Selective chelation of heavy metals is relevant to bioremediation (e.g., removal of Cs from radioactive waste).