Dissecting the Mechanism of Biosynthesis of Sulfurated Biomolecules: The Case of tRNA Sulfuration
Résumé
Sulfuration of biomolecules is a crucial biochemical process responsible for producing essential organic cofactors, coenzymes, vitamins, and other sulfurated biomolecules. In particular, thio-modified nucleosides in transfer RNA (tRNA) play a key role in ensuring the accuracy and efficiency of genetic translation. Although sulfurating enzymes have been studied structurally and biochemically since the early 2000s, detailed mechanistic analyses remain limited. In particular, the importance of reductants used in catalytic assays is often underappreciated.
In recent years, the use of anaerobic conditions has led to the discovery, in many of these enzymes, of an air-sensitive iron-sulfur cluster that is essential for catalysis. This led to the proposal of a catalytic mechanism involving a [4Fe-5S] intermediate, distinct from the previously accepted persulfide-based pathway. As this remains a debated topic, the current understanding of both mechanisms and the role of reductants warrants critical evaluation.
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