ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Origin of the Kinetic Isotope Effect and Mechanism of H/D Exchange in Radical C-C Bond Formation Catalyzed by Benzylsuccinate Synthase: Experiments and Microkinetic Modeling.The journal of physical chemistry. B · 2026Article
- Putative Mechanisms for Initial Reaction of Anaerobic Benzene Degradation Presumably Involving a Flavoprotein.Environmental microbiology · 2026Article
- Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.Biochemistry · 2026Review
- The Structural Basis of Malodorant Skatole Formation by the Glycyl Radical Enzyme Indoleacetate Decarboxylase.bioRxiv : the preprint server for biology · 2026Article
- Unravelling the Enantioselective Mechanism of Benzylsuccinate Synthase: Insights into Anaerobic Hydrocarbon Degradation through Multiscale Modeling and Microkinetics.Biochemistry · 2026Article
- Chymotrypsin digestion analysis of glycyl radical and B12-dependent radical enzymes indicates common substrate-induced structural shifts.Scientific reports · 2025Article
- Article
- Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Activation of X-Succinate Synthases for Fumarate Hydroalkylation Using an In Vitro Activation Method.Bio-protocol · 2025Article
- Modeling the Initiation Phase of the Catalytic Cycle in the Glycyl-Radical Enzyme Benzylsuccinate Synthase.The journal of physical chemistry. B · 2024Article
- A Synthetic Pathway for the Production of Benzylsuccinate inMolecules (Basel, Switzerland) · 2024Article
- Development of aniScience · 2023Article
- Activation of Glycyl Radical Enzymes─Multiscale Modeling Insights into Catalysis and Radical Control in a Pyruvate Formate-Lyase-Activating Enzyme.Journal of chemical information and modeling · 2022Article
- Parameter Reliability and Understanding Enzyme Function.Molecules (Basel, Switzerland) · 2022Review
- Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.Cell chemical biology · 2021Article
- A benzoxazole derivative as an inhibitor of anaerobic choline metabolism by human gut microbiota.RSC medicinal chemistry · 2020Article
- Discovery of CC bond-forming and bond-breaking radical enzymes: enabling transformations for metabolic engineering.Current opinion in biotechnology · 2020Review
- Benzylsuccinate Synthase is Post-Transcriptionally Regulated in the Toluene-Degrading DenitrifierMicroorganisms · 2020Article
- New Frontiers of Anaerobic Hydrocarbon Biodegradation in the Multi-Omics Era.Frontiers in microbiology · 2020Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Anaerobic degradation of the environmental pollutant toluene is initiated by the glycyl radical enzyme benzylsuccinate synthase (BSS), which catalyzes the radical addition of toluene to fumarate, forming benzylsuccinate. We have determined crystal structures of the catalytic α-subunit of BSS with its accessory subunits β and γ, which both bind a [4Fe-4S] cluster and are essential for BSS activity in vivo. We find that BSSα has the common glycyl radical enzyme fold, a 10-stranded β/α-barrel that surrounds the glycyl radical cofactor and active site. Both accessory subunits β and γ display folds related to high potential iron-sulfur proteins but differ substantially from each other in how they interact with the α-subunit. BSSγ binds distally to the active site, burying a hydrophobic region of BSSα, whereas BSSβ binds to a hydrophilic surface of BSSα that is proximal to the active site. To further investigate the function of BSSβ, we determined the structure of a BSSαγ complex. Remarkably, we find that the barrel partially opens, allowing the C-terminal region of BSSα that houses the glycyl radical to shift within the barrel toward an exit pathway. The structural changes that we observe in the BSSαγ complex center around the crucial glycyl radical domain, thus suggesting a role for BSSβ in modulating the conformational dynamics required for enzyme activity. Accompanying proteolysis experiments support these structural observations.
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