Presentation Title

Structural Analysis of Two Monooxygenases Involved in the Sulfur Metabolism Pathway of Gordonia sp. NB4-1Y

Format of Presentation

Poster to be presented the Friday of the conference

Presenter Information

Mathew NormanFollow

Abstract

6:2 fluorotelomer sulfonate (6:2 FTS) is a surfactant commonly used in fire fighting foams, although the compound poses a toxic threat in environmental conditions at higher concentrations. Many polyfluorinated alkyl (PFA) substances, such as 6:2 FTS, do not undergo spontaneous degradation under environmental conditions and therefore bio-accumulate in terrestrial and aquatic ecosystems. However, bacteria such as Gordonia sp. NB41Y have displayed bio-remediation potential for these contaminants, utilizing a sulfur metabolism pathway which is demonstrated to break down 6:2 FTS. Our research takes an X-ray crystallography approach to structurally characterize two key monooxygenase enzymes (ISGA1218 and ISGA1222) in this metabolic pathway. So far, the predicted structures of the enzymes has been generated and computational comparisons have been carried out with the closest structure and sequence homologs, while various screens are being tested to generate crystals for X-ray analysis. There are no known X-ray structures present for either of the enzymes and probing the molecular interactions between these enzymes and 6:2 FTS is an excellent start to elucidating this novel process. This research will not only aid our understanding of the structural basis of substrate recognition and the structure-function relationships for the enzymes, but also provide foundational understanding of enzymatic interactions with polyfluorinated alkyl substances for future industrial bio-remediation initiatives.

Department

Biological Sciences

Faculty Advisor

Jonathan Van Hamme and Chelsea Vickers

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Structural Analysis of Two Monooxygenases Involved in the Sulfur Metabolism Pathway of Gordonia sp. NB4-1Y

6:2 fluorotelomer sulfonate (6:2 FTS) is a surfactant commonly used in fire fighting foams, although the compound poses a toxic threat in environmental conditions at higher concentrations. Many polyfluorinated alkyl (PFA) substances, such as 6:2 FTS, do not undergo spontaneous degradation under environmental conditions and therefore bio-accumulate in terrestrial and aquatic ecosystems. However, bacteria such as Gordonia sp. NB41Y have displayed bio-remediation potential for these contaminants, utilizing a sulfur metabolism pathway which is demonstrated to break down 6:2 FTS. Our research takes an X-ray crystallography approach to structurally characterize two key monooxygenase enzymes (ISGA1218 and ISGA1222) in this metabolic pathway. So far, the predicted structures of the enzymes has been generated and computational comparisons have been carried out with the closest structure and sequence homologs, while various screens are being tested to generate crystals for X-ray analysis. There are no known X-ray structures present for either of the enzymes and probing the molecular interactions between these enzymes and 6:2 FTS is an excellent start to elucidating this novel process. This research will not only aid our understanding of the structural basis of substrate recognition and the structure-function relationships for the enzymes, but also provide foundational understanding of enzymatic interactions with polyfluorinated alkyl substances for future industrial bio-remediation initiatives.