Mitigating product inhibition in 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB) with synthetic glycosylation.

ABSTRACT: The combustion of sulfur-rich crude oil is toxic to the environment, making the removal of sulfur impurities a priority for the sustainable use of liquid fuels. Biodesulfurization via the 4S pathway is a promising approach due to its C-S bond cleavage specificity and mild operating conditions. However, biodesulfurization is not economically viable due to the slow turnover of 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB), an enzyme catalyzing the conversion of 2'-hydroxybiphenyl-2-sulfinate to 2-hydroxybiphenyl and sulfite. Previous studies have identified product inhibition as the limiting factor in DszB, whereby solvent-exposed protein loops obstruct the active site after substrate binding. This closed conformation is stabilized by hydrophobic interactions between the loops and the pr

SUBMITTER: Liang J 

PROVIDER: S-EPMC12168087 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature