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Sulfur-based ligands, principally cysteinate, methionine and sulfide, are found in many metallo­enzymes. As these enzymes operate in a protic environment and (in some cases) involve substrates being transformed by sequences of electron and proton transfer reactions, it is important to understand the protonation chemistry of these sulfur-based ligands. In this review, the mechanisms and proton transfer rates of both coordinated thiolates and sulfides are presented, with a particular emphasis on synthetic Fe-S-based clusters. The protonation of natural Fe-S-based clusters is considered in the light of the studies on the synthetic models.

Rates of protonation of thiolate and sulfide ligands in mononuclear complexes and Fe-S-based clusters: implications for metalloenzymes