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  • OvoA Mtht from Methyloversatilis thermotolerans ovothiol biosynthesis is a bifunction enzyme: thiol oxygenase and sulfoxide synthase activities
Title: OvoA Mtht 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.  more » « less
Award ID(s):
1654060
PAR ID:
10324051
Author(s) / Creator(s):
; ; ; ; ; ; ; ; ; ; ; ; ; ;
Date Published:
Journal Name:
Chemical Science
Volume:
13
Issue:
12
ISSN:
2041-6520
Page Range / eLocation ID:
3589 to 3598
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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