2024 article
New Frontiers in Nonheme Enzymatic Oxyferryl Species
Paris, J. C., Cheung, Y. H., Zhang, T., Chang, W.-chen, Liu, P., & Guo, Y. (2024, August 7). CHEMBIOCHEM.
author keywords: Ferryl intermediates; Nonheme iron enzymes; Spin state; Oxidative C-S bond formation; C-H activation
open access via doi.org (publisher)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 19, 2024
Abstract Non‐heme mononuclear iron dependent (NHM−Fe) enzymes exhibit exceedingly diverse catalytic reactivities. Despite their catalytic versatilities, the mononuclear iron centers in these enzymes show a relatively simple architecture, in which an iron atom is ligated with 2–4 amino acid residues, including histidine, aspartic or glutamic acid. In the past two decades, a common high‐valent reactive iron intermediate, the S =2 oxyferryl (Fe(IV)‐oxo or Fe(IV)=O) species, has been repeatedly discovered in NHM−Fe enzymes containing a 2‐His‐Fe or 2‐His‐1‐carboxylate‐Fe center. However, for 3‐His/4‐His‐Fe enzymes, no common reactive intermediate has been identified. Recently, we have spectroscopically characterized the first S =1 Fe(IV) intermediate in a 3‐His‐Fe containing enzyme, OvoA, which catalyzes a novel oxidative carbon‐sulfur bond formation. In this review, we summarize the broad reactivities demonstrated by S =2 Fe(IV)‐oxo intermediates, the discovery of the first S =1 Fe(IV) intermediate in OvoA and the mechanistic implication of such a discovery, and the intrinsic reactivity differences of the S =2 and the S =1 Fe(IV)‐oxo species. Finally, we postulate the possible reasons to utilize an S =1 Fe(IV) species in OvoA and their implications to other 3‐His/4‐His‐Fe enzymes.