Abstract
The alkanesulfonate monooxygenase system from Pseudomonas putida enables the organism to utilize sulfonates and sulfate esters from the environment. The alkanesulfonate monooxygenase system is comprised of an FMN reductase (SsuE) and flavin‐dependent monooxygenase (SsuD). Although this system from Escherichia coli has been studied, the alkanesulfonate system from P. putida has not been evaluated. The system in P. putida possesses a third protein, SsuF, but the role of SsuF in the desulfonation mechanism has not been determined. SsuF has shown to have a high identity to a molybdopterin binding protein within E. coli. Previous studies have shown that SsuF is required for growth with sulfate esters and sulfonates, but the exact function of this protein has not been determined.As P. putida possesses the additional SsuF protein, it is possible that the alkanesulfonate monooxygenase system may operate under an alternative mechanism than the E. coli system. Following the expression and purification of SsuF, several spectroscopic techniques were employed to analyze the structural and functional characteristics of the proteins. Further evaluation of SsuF was performed to determine the substrate range of SsuD and SsuE in the presence and absence of SsuF. Based on these studies, a functional role for SsuF in the desulfonation mechanism has been established.Work supported by NSF Grant MCB545048.
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