What does this research mean for the field?

Sulfoquinovose dioxygenase (SqoD) facilitates bacterial carbon assimilation from sulfoquinovose by cleaving C–S bonds using an Fe(II)/α-ketoglutarate mechanism. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

To investigate the structural and mechanistic aspects of sulfoquinovose dioxygenase (SqoD) facilitating C–S bond cleavage.

February 26, 2026Chemical Science2 citationsOpen Access

Structural and mechanistic basis of sulfolytic C–S bond cleavage by an Fe(II)/α-ketoglutarate-dependent sulfoquinovose dioxygenase

MLMihwa LeeThe University of Melbourne HHHo NN HoThe University of Melbourne MMmegan Maher

Key Points

To investigate the structural and mechanistic aspects of sulfoquinovose dioxygenase (SqoD) facilitating C–S bond cleavage.
Determined crystal structures of SqoD from Marinobacterium aestuarii
Analyzed the interaction between Fe(II) and α-ketoglutarate in the cleavage process
Identified key structural features of SqoD involved in enzymatic function
Demonstrated the pathway of carbon assimilation through the cleavage of the C–S bond

Abstract

Sulfoquinovose dioxygenase (SqoD) enables bacterial carbon assimilation from the abundant sulfosugar sulfoquinovose (SQ) by Fe(II)/α-ketoglutarate (αKG)–dependent C–S bond cleavage. Here we report crystal structures of the Marinobacterium aestuarii enzyme ( Ma SqoD)...

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