The nature of heme-thiolate proteins is influenced by secondary interactions between the cysteine sulfur atom and a peptide-derived N�H moiety. For example, investigations of both heme-thiolate proteins and model complexes have demonstrated an increase in heme iron redox potential with increasing hydrogen bonding. Additionally, we hypothesize that these NH���S type hydrogen bonds play a critical role in determining the function (either catalytic or sensory) of heme-thiolate proteins. Thus, we wish to synthesize six-coordinate, low-spin heme-thiolate model complexes and explore the effect of hydrogen bonding on the electronic structure and reactivity of these centers. Here, we report novel preparations of 2-(acetylamino)thiophenolate and 2,6-bis(acetylamino)thiophenolate derivatives, ligands that will donate one and two hydrogen bonds to a heme-bound thiolate, respectively. We also report syntheses of 2-(acetoxy)thiophenolate and 2,6-bis(acetoxy)thiophenolate derivatives, ligands which control for the steric bulk of the NH���S bonding ligands.

Novel preparations of thiophenol derivatives to model heme-thiolate NH���S hydrogen bonding

248th National Meeting (2014)

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Novel preparations of thiophenol derivatives to model heme-thiolate NH���S hydrogen bonding

Novel preparations of thiophenol derivatives to model heme-thiolate NH��S hydrogen bonding