Abstract
A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to effect substrate oxidations that range from the hydroxylation of methane and the desaturation of fatty acids to the deformylation of fatty aldehydes to produce alkanes and the six-electron oxidation of aminoarenes to nitroarenes in the biosynthesis of antibiotics. A common feature of their reaction mechanisms is the formation of O2 adducts that evolve into more reactive derivatives such as diiron(II,III)-superoxo, diiron(III)-peroxo, diiron(III,IV)-oxo, and diiron(IV)-oxo species, which carry out particular substrate oxidation tasks. In this review, we survey the various enzymes belonging to this unique subset and the mechanisms by which substrate oxidation is carried out. We examine the nature of the reactive intermediates, as revealed by X-ray crystallography and the application of various spectroscopic methods and their associated reactivity. We also discuss the structural and electronic properties of the model complexes that have been found to mimic salient aspects of these enzyme active sites. Much has been learned in the past 25 years, but key questions remain to be answered.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2554-2592 |
| Number of pages | 39 |
| Journal | Chemical Reviews |
| Volume | 118 |
| Issue number | 5 |
| DOIs | |
| State | Published - Mar 14 2018 |
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Dioxygen Activation by Nonheme Diiron Enzymes : Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes. / Jasniewski, Andrew J.; Que, Lawrence.
In: Chemical Reviews, Vol. 118, No. 5, 14.03.2018, p. 2554-2592.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dioxygen Activation by Nonheme Diiron Enzymes
T2 - Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes
AU - Jasniewski, Andrew J.
AU - Que, Lawrence
PY - 2018/3/14
Y1 - 2018/3/14
N2 - A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to effect substrate oxidations that range from the hydroxylation of methane and the desaturation of fatty acids to the deformylation of fatty aldehydes to produce alkanes and the six-electron oxidation of aminoarenes to nitroarenes in the biosynthesis of antibiotics. A common feature of their reaction mechanisms is the formation of O2 adducts that evolve into more reactive derivatives such as diiron(II,III)-superoxo, diiron(III)-peroxo, diiron(III,IV)-oxo, and diiron(IV)-oxo species, which carry out particular substrate oxidation tasks. In this review, we survey the various enzymes belonging to this unique subset and the mechanisms by which substrate oxidation is carried out. We examine the nature of the reactive intermediates, as revealed by X-ray crystallography and the application of various spectroscopic methods and their associated reactivity. We also discuss the structural and electronic properties of the model complexes that have been found to mimic salient aspects of these enzyme active sites. Much has been learned in the past 25 years, but key questions remain to be answered.
AB - A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to effect substrate oxidations that range from the hydroxylation of methane and the desaturation of fatty acids to the deformylation of fatty aldehydes to produce alkanes and the six-electron oxidation of aminoarenes to nitroarenes in the biosynthesis of antibiotics. A common feature of their reaction mechanisms is the formation of O2 adducts that evolve into more reactive derivatives such as diiron(II,III)-superoxo, diiron(III)-peroxo, diiron(III,IV)-oxo, and diiron(IV)-oxo species, which carry out particular substrate oxidation tasks. In this review, we survey the various enzymes belonging to this unique subset and the mechanisms by which substrate oxidation is carried out. We examine the nature of the reactive intermediates, as revealed by X-ray crystallography and the application of various spectroscopic methods and their associated reactivity. We also discuss the structural and electronic properties of the model complexes that have been found to mimic salient aspects of these enzyme active sites. Much has been learned in the past 25 years, but key questions remain to be answered.
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UR - http://www.scopus.com/inward/citedby.url?scp=85043781316&partnerID=8YFLogxK
U2 - 10.1021/acs.chemrev.7b00457
DO - 10.1021/acs.chemrev.7b00457
M3 - Article
C2 - 29400961
AN - SCOPUS:85043781316
VL - 118
SP - 2554
EP - 2592
JO - Chemical Reviews
JF - Chemical Reviews
SN - 0009-2665
IS - 5
ER -