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Chem Rev. 2017 Nov 08;117(21):13320-13352. doi: 10.1021/acs.chemrev.7b00180. Epub 2017 Oct 09.

Biomimetic Reactivity of Oxygen-Derived Manganese and Iron Porphyrinoid Complexes.

Chemical reviews

Regina A Baglia, Jan Paulo T Zaragoza, David P Goldberg

Affiliations

  1. Department of Chemistry, The Johns Hopkins University , 3400 North Charles Street, Baltimore, Maryland 21218, United States.

PMID: 28991451 PMCID: PMC6058703 DOI: 10.1021/acs.chemrev.7b00180

Abstract

Heme proteins utilize the heme cofactor, an iron porphyrin, to perform a diverse range of reactions including dioxygen binding and transport, electron transfer, and oxidation/oxygenations. These reactions share several key metalloporphyrin intermediates, typically derived from dioxygen and its congeners such as hydrogen peroxide. These species are composed of metal-dioxygen, metal-superoxo, metal-peroxo, and metal-oxo adducts. A wide variety of synthetic metalloporphyrinoid complexes have been synthesized to generate and stabilize these intermediates. These complexes have been studied to determine the spectroscopic features, structures, and reactivities of such species in controlled and well-defined environments. In this Review, we summarize recent findings on the reactivity of these species with common porphyrinoid scaffolds employed for biomimetic studies. The proposed mechanisms of action are emphasized. This Review is organized by structural type of metal-oxygen intermediate and broken into subsections based on the metal (manganese and iron) and porphyrinoid ligand (porphyrin, corrole, and corrolazine).

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