Proteins which contain a heme cofactor bound to a cysteine residue are categorized as thiolate-ligated heme proteins. Certain thiolate-ligated heme proteins can switch protein-derived ligands upon reduction of the heme iron and this switch appears to be a method of regulation. In an attempt to better understand these proteins, a series of model proteins have been generated by creating mutations in yeast iso-1-cytochrome <i>c</i> that permit cysteine ligation to the heme. Previous research has shown that the heme absorbance spectrum changes upon reduction of the heme, suggesting a change has occurred in the heme environment. A variety of chemical and spectroscopic tests were performed to investigate the redox-dependent heme environment of the model proteins and the results of these experiments will be discussed.

Studying the effect of redox environment on heme ligation in Cys80 variants of iso-1-cytochrome <i>c</i>

251st National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Studying the effect of redox environment on heme ligation in Cys80 variants of iso-1-cytochrome c