Hydrogen Peroxide Dependent <i>cis</i>-Dihydroxylation of Benzoate by Fully Oxidized Benzoate 1,2-Dioxygenase

Neibergall, Matthew B.; Stubna, Audria; Mekmouche, Yasmina; Münck, Eckard; Lipscomb, John D.

doi:10.1021/bi700120j

Cited by 85 publications

(129 citation statements)

References 39 publications

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“…[19,158,159] Similar results were obtained experimentally [223] for the nucleophilic (deformylation of aldehydes)…”

Section: Mononuclear Ferric-peroxo and Ferric-hydroperoxo Active Sitesupporting

confidence: 81%

“…[45] On the other hand, the high-spin (S = 5/2) Fe III ─OOH intermediate, proposed to be formed in Rieske dioxygenases (RDO), [157,158,159] should have oxidant ability in electrophilic aromatic substitution reactions (note that alternative intermediates in RDO were also proposed [160,161] Figure 2) was crystallographically defined only as late as in 2014. [165] This synthetic system was shown to undergo both an aliphatic C─H activation and nucleophilic oxidation reaction.…”

Section: Mononuclear Ferric-hydroperoxo Active Site: C─h + Hoo─fe IIImentioning

confidence: 99%

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Mono- and binuclear non-heme iron chemistry from a theoretical perspective

et al. 2016

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In this minireview, we provide an account of the current state-of-the-art developments in the area of mono-and binuclear non-heme enzymes (NHFe and NHFe2) and the smaller NHFe(2) synthetic models, mostly from a theoretical and computational perspective. The sheer complexity, and at the same time the beauty, of the NHFe(2) world represent a challenge for both experimental as well as theoretical methods. We emphasize that the concerted progress on both theoretical and experimental side is a conditio sine qua non for future understanding, exploration and utilization of the NHFe(2) systems.After briefly discussing the current challenges and advances in the computational methodology, we review the recent spectroscopic and computational studies of NHFe(2) enzymatic and inorganic systems and highlight the correlations between various experimental data (spectroscopic, kinetic, thermodynamic, electrochemical) and computations. Throughout, we attempt to keep in mind the most fascinating and attractive phenomenon in the NHFe(2) chemistry which is the fact that despite the strong oxidative power of many reactive intermediates, the NHFe(2) enzymes perform catalysis with high selectivity. We conclude with our personal viewpoint and hope that further developments in quantum chemistry and especially in the field of multireference wave function methods are needed to have a solid theoretical basis for the NHFe(2) studies, mostly by providing benchmarking and calibration of the computationally efficient and easy-to-use DFT methods.

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“…[19,158,159] Similar results were obtained experimentally [223] for the nucleophilic (deformylation of aldehydes)…”

Section: Mononuclear Ferric-peroxo and Ferric-hydroperoxo Active Sitesupporting

confidence: 81%

Section: Mononuclear Ferric-hydroperoxo Active Site: C─h + Hoo─fe IIImentioning

confidence: 99%

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

et al. 2016

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“…Mössbauer spectrum and simulation (red) of the nearly EPR silent intermediate after 4 min of reaction. Adapted from reference 27 .…”

Section: Discussionmentioning

confidence: 99%

Finding Intermediates in the O₂ Activation Pathways of Non-Heme Iron Oxygenases

et al. 2007

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Intermediates in the reaction cycle of an oxygenase are usually very informative of the chemical mechanism of O 2 activation and insertion. However, detection of these intermediates is often complicated by their short lifetime and the regulatory mechanism of the enzyme designed to ensure specificity. Here, the methods used to detect the intermediates in an extradiol dioxygenase, a Rieske cis-dihydrodiol dioxygenase, and soluble methane monooxygenase are discussed. The methods include the use of alternative, chromophoric substrates, mutagenesis of active site catalytic residues, forced changes in substrate binding order, control of reaction rates using regulatory proteins, and initialization of catalysis in crystallo.

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“…Both mechanistic scenarios have received support from computational studies 48,49 . One direct approach to resolving this controversy has been to show that hydrogen peroxide added to the substrate complex of naphthalene or benzoate dioxygenase (BZDO) in the resting state with the Rieske cluster oxidized and the mononuclear iron reduced yields nearly stoichiometric amounts of product (a peroxide shunt) 50,51 . In this case, 18 O-labeling studies showed the peroxide is the source of the oxygen in the product, and because it can supply only two electrons, the two-electron activated oxygen proposal is favored.…”

Section: Rieske Cis-diol Forming Dioxygenasesmentioning

confidence: 99%

“…In this case, 18 O-labeling studies showed the peroxide is the source of the oxygen in the product, and because it can supply only two electrons, the two-electron activated oxygen proposal is favored. In the case of BZDO, a form with both the Rieske and mononuclear iron sites fully oxidized was prepared, and this state was also active in the peroxide shunt despite the lack of any source for a third electron 51 .…”

Section: Rieske Cis-diol Forming Dioxygenasesmentioning

confidence: 99%

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions

2008

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Oxidase and oxygenase enzymes allow the use of relatively unreactive O 2 in biochemical reactions. Many of the mechanistic strategies employed in nature for this key reaction are represented within the 2-His-1-carboxylate facial triad family of non-heme Fe(II) containing enzymes. The open face of the metal coordination sphere opposite the three endogenous ligands participates directly in the reaction chemistry. Here, data from several studies are presented showing that reductive O 2 activation within this family is initiated by substrate (and in some cases co-substrate or cofactor) binding, which then allows coordination of O 2 to the metal. From this starting point, both the O 2 activation process and the reactions with substrates diverge broadly. The reactive species formed in these reactions have been proposed to encompass four oxidation states of iron and all forms of reduced O 2 as well as several of the reactive oxygen species that derive from O-O bond cleavage.Dioxygen serves at least three quite different roles that profoundly impact aerobic life. The most commonly appreciated role is to serve as the terminal electron acceptor in processes such as oxidative phosphorylation that yield the central energy-rich molecules used throughout metabolism. The second, no less important role is to serve as the source for many of the oxygen atoms found in the essential molecules of biological systems such as steroid hormones, aromatic amino acids, neurotransmitters, signalling molecules, and regulatory factors 1 . Also, processes operating on a global scale, such as the recovery of the enormous quantities of carbon sequestered as lignin in plant life or the oxidation of the billions of tons of methane generated by anaerobes before it can enter the atmosphere, also involve oxygen incorporation from O 2 2 ,3 . On a more local scale, biodegradation of both aliphatic and aromatic toxic compounds often begins with the incorporation of oxygen 4 . The third, and least appreciated role played by dioxygen in aerobic organisms involves neither energy conversion nor oxygen incorporation. Rather, some enzymes can convert dioxygen to alternative forms that are, in effect, highly specialized reagents that are used to catalyze the synthesis of important biomolecules. An excellent example of the latter role for O 2 is the biosynthesis of penicillintype antibiotics 5,6 , which is discussed in more detail later in this review.Dioxygen is an attractive reagent for use in a biological system because its high potential reactivity is held in check by its molecular structure. The triplet ground state of O 2 that results from the presence of two unpaired electrons in degenerate molecular orbitals makes the direct reaction with singlet molecules, the spin-paired state of most potential reaction partners, a forbidden process 7 . The central question that has faced chemists and biochemists for the half Competing Interests StatementThe authors declare no competing financial interests. Of course, the answers to this question are of fundam...

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Hydrogen Peroxide Dependent cis-Dihydroxylation of Benzoate by Fully Oxidized Benzoate 1,2-Dioxygenase

Cited by 85 publications

References 39 publications

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

Finding Intermediates in the O₂ Activation Pathways of Non-Heme Iron Oxygenases

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions

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Hydrogen Peroxide Dependent cis-Dihydroxylation of Benzoate by Fully Oxidized Benzoate 1,2-Dioxygenase

Cited by 85 publications

References 39 publications

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

Finding Intermediates in the O2 Activation Pathways of Non-Heme Iron Oxygenases

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions

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Finding Intermediates in the O₂ Activation Pathways of Non-Heme Iron Oxygenases