Journal
CHEMICAL REVIEWS
Volume 117, Issue 21, Pages 13320-13352Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrev.7b00180
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Funding
- NIH [GM101153]
- Harry and Cleio Greer Fellowship
- Glen E. Meyer '39 Fellowship
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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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