The metal-sulfur bonds of many metalloproteins are influenced by NH���S type hydrogen bonds formed between a cysteine sulfur atom and an N�H group from the peptide backbone or a nearby amino acid side chain. For example, in the electron transport protein rubredoxin, the four cysteine sulfur atoms that coordinate the iron atom are involved in hydrogen bonding with the protein backbone. A correlation between redox potential and the amount of NH���S hydrogen bonding has been demonstrated through work with rubredoxin model complexes. The cysteine sulfur coordinated to the heme iron of Cytochrome P450cam is also engaged in NH���S hydrogen bonding with the backbone N�H groups of neighboring residues. Mutation studies and investigations of model complexes have demonstrated an increase in heme redox potential with increasing hydrogen bonding in this system. To further investigate the effects of hydrogen bonding on metal centers similar to those present in iron-sulfur metalloproteins, a series of 2,6-bis(acetylaminomethyl)thiophenolate ligand derivatives have been synthesized. In constrast to previously studied 2,6-bis(acetylamino)thiophenolate derivatives, addition of the methylene group adjacent to the ring allows for an optimized NH���S orientation.

Progress towards metal-thiolate model complexes incorporating 2,6-bis(acetylaminomethyl)thiophenol derivatives to model biological NH���S hydrogen bonding

246th National Meeting (2013)

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Progress towards metal-thiolate model complexes incorporating 2,6-bis(acetylaminomethyl)thiophenol derivatives to model biological NH���S hydrogen bonding

Progress towards metal-thiolate model complexes incorporating 2,6-bis(acetylaminomethyl)thiophenol derivatives to model biological NH��S hydrogen bonding