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Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.

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.

SUBMITTER: Jasniewski AJ

PROVIDER: S-EPMC5920527 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

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Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.

Jasniewski Andrew J AJ Que Lawrence L

Chemical reviews 20180205 5

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 O<sub>2</sub> adducts that evolve into more reactive derivatives such as diiron ...[more]

PMID: 29400961

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Project description:To obtain structural and spectroscopic models for the diiron(II,III) centers in the active sites of diiron enzymes, the (μ-alkoxo)(μ-carboxylato)diiron(II,III) complexes [Fe(II)Fe(III)(N-Et-HPTB)(O(2)CPh)(NCCH(3))(2)](ClO(4))(3) (1) and [Fe(II)Fe(III)(N-Et-HPTB)(O(2)CPh)(Cl)(HOCH(3))](ClO(4))(2) (2) (N-Et-HPTB = N,N,N',N'-tetrakis(2-(1-ethyl-benzimidazolylmethyl))-2-hydroxy-1,3-diaminopropane) have been prepared and characterized by X-ray crystallography, UV-visible absorption, EPR, and Mössbauer spectroscopies. Fe1-Fe2 separations are 3.60 and 3.63 Å, and Fe1-O1-Fe2 bond angles are 128.0° and 129.4° for 1 and 2, respectively. Mössbauer and EPR studies of 1 show that the Fe(III) (S(A) = 5/2) and Fe(II) (S(B) = 2) sites are antiferromagnetically coupled to yield a ground state with S = 1/2 (g= 1.75, 1.88, 1.96); Mössbauer analysis of solid 1 yields J = 22.5 ± 2 cm(-1) for the exchange coupling constant (H = JS(A)·S(B) convention). In addition to the S = 1/2 ground-state spectrum of 1, the EPR signal for the S = 3/2 excited state of the spin ladder can also be observed, the first time such a signal has been detected for an antiferromagnetically coupled diiron(II,III) complex. The anisotropy of the (57)Fe magnetic hyperfine interactions at the Fe(III) site is larger than normally observed in mononuclear complexes and arises from admixing S > 1/2 excited states into the S = 1/2 ground state by zero-field splittings at the two Fe sites. Analysis of the "D/J" mixing has allowed us to extract the zero-field splitting parameters, local g values, and magnetic hyperfine structural parameters for the individual Fe sites. The methodology developed and followed in this analysis is presented in detail. The spin Hamiltonian parameters of 1 are related to the molecular structure with the help of DFT calculations. Contrary to what was assumed in previous studies, our analysis demonstrates that the deviations of the g values from the free electron value (g = 2) for the antiferromagnetically coupled diiron(II,III) core in complex 1 are predominantly determined by the anisotropy of the effective g values of the ferrous ion and only to a lesser extent by the admixture of excited states into ground-state ZFS terms (D/J mixing). The results for 1 are discussed in the context of the data available for diiron(II,III) clusters in proteins and synthetic diiron(II,III) complexes.

Dataset Information

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.

Publications

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.

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