Exploring the Effects of Hydrogen Bonding on Hydrosulfide Desulfurization in Carbonic Anhydrase Using Synthetic Modeling Approach
Carbonic anhydrase (CA) is a metalloprotein that is commonly found in animals, plants, algae, and bacteria. Carbonic anhydrase catalyzes the reversible hydration of carbon dioxide into bicarbonate ions, and also can react with carbonyl sulfide (COS) to generate hydrogen sulfide (H2S). However, the mechanism of carbonyl sulfide activation is not fully understood. The focus of our research is to a) determine the factors necessary for desulfurization of the zinc-hydrosulfide intermediate formed in the catalytic process and b) how desulfurization occurs near a physiological pH. In particular, we want to determine if hydrogen bonding interactions have an effect on influencing the protonation and desulfurization of the hydrosulfide group. As such, two zinc-hydrosulfide complexes (one complex lacks a hydrogen bond donor and the other contains a single hydrogen bond donor) have been prepared and the pH where desulfurization occurs measured. The results of this study and the effect hydrogen bonding had on hydrosulfide desulfurization will be presented.
Volz, Lillian, "Exploring the Effects of Hydrogen Bonding on Hydrosulfide Desulfurization in Carbonic Anhydrase Using Synthetic Modeling Approach" (2016). 2016 Undergraduate Research and Scholarship Conference. Paper 71.