Carbonic anhydrase (CA) is a zinc metalloenzyme that hydrates carbon dioxide to form bicarbonate with remarkable efficiency. Because CA acts not only on CO2, but also on the heterocumulenes COS and CS2, this enzyme is interesting for its potential role in the sequestration and transport of these gases. Reaction with sulfur-containing heterocumulenes leads, however, to formation of a zinc (II) hydrosulfide, rendering the enzyme inactive until the zinc-sulfur bond is cleaved.  It is currently unclear how the regeneration occurs, although several pathways present themselves as plausible.  To better understand this cycle, low molecular weight synthetic models built around a copper or zinc center, both of which mimic the active site of CA, have been synthesized and their behavior with carbon disulfide examined.  This work has led to the synthesis of the first reported copper (II) hydrosulfide as well as the first observed case of a �-sulfide bridging two zinc centers.

Understanding the mechanism of action of carbonic anhydrase
on heterocumulenes using synthetic models

239th National Meeting (2010)

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Understanding the mechanism of action of carbonic anhydrase on heterocumulenes using synthetic models