Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum

Jinling Li; Mahima Sharma; Richard Meek; Amani Alhifthi; Zachary Armstrong; Niccolay Madiedo Soler; Mihwa Lee; Ethan D. Goddard-Borger; James N. Blaza; Gideon J. Davies; Spencer J. Williams

doi:10.1039/D3SC01594G

Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum†

Jinling Li,^a Mahima Sharma,

^b Richard Meek,

^b Amani Alhifthi,^ac Zachary Armstrong,^a Niccolay Madiedo Soler,^d Mihwa Lee,^a Ethan D. Goddard-Borger,^de James N. Blaza,^b Gideon J. Davies

*^b and Spencer J. Williams

*^a

Author affiliations

* Corresponding authors

^a School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia
E-mail: sjwill@unimelb.edu.au

^b York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, UK
E-mail: gideon.davies@york.ac.uk

^c Chemistry Department, Faculty of Science (Female Section), Jazan University, Jazan 82621, Saudi Arabia

^d ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3010, Australia

^e Department of Medical Biology, University of Melbourne, Parkville, Victoria 3010, Australia

Abstract

Sulfolactate (SL) is a short-chain organosulfonate that is an important reservoir of sulfur in the biosphere. SL is produced by oxidation of sulfolactaldehyde (SLA), which in turn derives from sulfoglycolysis of the sulfosugar sulfoquinovose, or through oxidation of 2,3-dihydroxypropanesulfonate. Oxidation of SLA is catalyzed by SLA dehydrogenases belonging to the aldehyde dehydrogenase superfamily. We report that SLA dehydrogenase RlGabD from the sulfoglycolytic bacterium Rhizobium leguminsarum SRDI565 can use both NAD⁺ and NADP⁺ as cofactor to oxidize SLA, and indicatively operates through a rapid equilibrium ordered mechanism. We report the cryo-EM structure of RlGabD bound to NADH, revealing a tetrameric quaternary structure and supporting proposal of organosulfonate binding residues in the active site, and a catalytic mechanism. Sequence based homology searches identified SLA dehydrogenase homologs in a range of putative sulfoglycolytic gene clusters in bacteria predominantly from the phyla Actinobacteria, Firmicutes, and Proteobacteria. This work provides a structural and biochemical view of SLA dehydrogenases to complement our knowledge of SLA reductases, and provide detailed insights into a critical step in the organosulfur cycle.

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Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum†

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