Which is the real oxidant in competitive ligand self-hydroxylation and substrate oxidation—a biomimetic iron(<scp>ii</scp>)-hydroperoxo species or an oxo-iron(<scp>iv</scp>)-hydroxy one?-Reference-Cited by-同舟云学术

Which is the real oxidant in competitive ligand self-hydroxylation and substrate oxidation—a biomimetic iron(ii)-hydroperoxo species or an oxo-iron(iv)-hydroxy one?

Published:2022 Issue:19 Volume:51 Page:7571-7580
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Cao Xuanyu¹²,Song Huiling³,Li Xiao-Xi⁴^ORCID,Qiao Qing-An³,Zhao Yufen¹²^ORCID,Wang Yong¹²^ORCID

Affiliation:

1. Institute of Drug Discovery Technology, Ningbo University, Ningbo 315211, China

2. Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Ningbo University, Ningbo 315211, China

3. School of Chemistry and Materials Science, Ludong University, Yantai 264025, China

4. Institute of Molecular Science and Engineering, Institute of Frontier and Interdisciplinary Sciences, Shandong University, Qingdao 266237, China

Abstract

The biomimetic iron(ii)-hydroperoxo species prefers to decay to an oxo-iron(iv)-hydroxy one to exert substrate oxidations and ligand self-hydroxylation.

Funder

National Natural Science Foundation of China

Ningbo University

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/DT/D2DT00797E

Reference81 articles.

1. Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates

2. Dioxygen Activation and Catalytic Aerobic Oxidation by a Mononuclear Nonheme Iron(II) Complex

3. Reactivity of an Iron–Oxygen Oxidant Generated upon Oxidative Decarboxylation of Biomimetic Iron(II) α-Hydroxy Acid Complexes

4. Non-Heme Fe(IV)–Oxo Intermediates

5. Quantum Chemical Studies of Mechanisms for Metalloenzymes

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