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

Chemical Science 2026 Open access

Read full text
Authors: Mihwa Lee, Ho NN Ho, Megan J. Maher, Guy N. L. Jameson, Spencer J. Williams
DOI: 10.1039/d5sc09188h
Cited by: 2
References: 47

Abstract

·αKG·SQ complex and thereby curbing uncoupled reactions. Pre-steady-state stopped-flow data support the canonical Fe(iv)[double bond, length as m-dash]O chemistry of the dioxygenase and reveal an additional intermediate consistent with an enzyme-bound α-hydroxysulfonate or 6-dehydroglucose species. Together, these findings define the structural and mechanistic basis of sulfolytic SQ catabolism and illuminate the functional repertoire of Fe(ii)/αKG-dependent dioxygenases in organosulfur carbon assimilation.

Fields of Study & Subjects

Environmental Chemistry and Analysis Synthesis and Catalytic Reactions Microbial bioremediation and biosurfactants

Publication details

Journal / source
Chemical Science
Publisher
Royal Society of Chemistry (RSC)
Volume
17
Issue
16
Pages
8100–8107
Publication date
1 January 2026
Language
EN