Abstract
Biodesulfurization provides a method to remove the sulfur from organosulfur compounds found in petroleum. This multi‐step pathway is able to remove sulfur from dibenzothiophene (DBT), one of the most recalcitrant compounds found in petroleum and crude oil. A critical enzyme in this pathway is an aromatic desulfinase (DszB) that catalyzes the final rate‐limiting step of the desulfurization. The DszB enzyme from Nocardia asteroides A3H1 was overexpressed in E. coli, purified using Ni2+‐affinity chromatography and characterized kinetically. Kinetic assays revealed a sigmoidal response when the velocity was plotted against substrate concentration, calling into question the monomeric structure of the enzyme previously reported by crystallography studies. Size exclusion chromatography and cross‐linking experiments were conducted to further investigate the oligomerization of HPBS desulfinase. Attempts to further purify the enzyme using Co2+‐affinity chromatography provided further evidence that under certain conditions DszB may exhibit cooperativity.Support or Funding InformationJMU Department of Chemistry and Biochemistry Dr. Linette M. Watkins NSF Grant No. CHE‐1757874
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