OvoAMtht from Methyloversatilis thermotolerans ovothiol biosynthesis is a bifunction enzyme: thiol oxygenase and sulfoxide synthase activities

Mononuclear non-heme iron enzymes are a large class of enzymes catalyzing a wide-range of reactions. In this work, we report that a non-heme iron enzyme in Methyloversatilis thermotolerans, OvoA(Mtht,) has two different activities, as a thiol oxygenase and a sulfoxide synthase. When cysteine is presented as the only substrate, OvoA(Mtht) is a thiol oxygenase. In the presence of both histidine and cysteine as substrates, OvoA(Mtht) catalyzes the oxidative coupling between histidine and cysteine (a sulfoxide synthase). Additionally, we demonstrate that both substrates and the active site iron's secondary coordination shell residues exert exquisite control over the dual activities of OvoA(Mtht) (sulfoxide synthase vs. thiol oxygenase activities). OvoA(Mtht) is an excellent system for future detailed mechanistic investigation on how metal ligands and secondary coordination shell residues fine-tune the iron-center electronic properties to achieve different reactivities.

Automated summary

This work reports the dual activities of a non-heme iron enzyme OvoA(Mtht) in Methyloversatilis thermotolerans, acting as a thiol oxygenase and a sulfoxide synthase. The control of the enzyme's dual activities by the substrates and the active site iron's secondary coordination shell residues is demonstrated. This finding provides an excellent system for future mechanistic investigation on the modulation of iron-centers' electronic properties for different reactivities.