AI Article Synopsis
- The anaerobic degradation of toluene starts when its methyl group combines with fumarate, a process facilitated by a unique enzyme called (R)-benzylsuccinate synthase (BSS).
- BSS is made up of three subunits (α, β, and γ) and has extra cofactors that distinguish it from similar enzymes, specifically iron-sulfur (FeS) clusters.
- Studies show that BSS contains a couple of different types of FeS clusters, indicating some enzymes have varying amounts due to a degradation process, with the clusters likely residing in the β and γ subunits due to their structural features.
Article Abstract
The anaerobic degradation pathway of toluene is initiated by the addition of the methyl group of toluene to the double bond of fumarate. This reaction is catalyzed by a novel glycyl-radical enzyme, (R)-benzylsuccinate synthase (BSS). The enzyme consists of three subunits, α, β, and γ, and differs from most other glycyl-radical enzymes in having additional cofactors. We have purified a Strep-tagged nonactivated BSS from recombinant Escherichia coli and identified the additional cofactors as FeS clusters by UV/vis, EPR, and Mössbauer spectroscopy. Analysis of the metal content as well as the EPR and Mössbauer spectra indicated that BSS contains magnetically coupled low-potential [4Fe-4S] clusters. Several enzyme preparations showed differing amounts of [3Fe-4S] clusters that could be reconstituted to [4Fe-4S] clusters, indicating that they arise from partial decay of the initial [4Fe-4S] clusters. The most likely location of these FeS clusters in the enzyme are the small β and γ subunits, which are unique for the BSS subfamily of glycyl-radical enzymes and contain conserved cysteines as potential ligands.
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