A new microperoxidase from Marinobacter hydrocarbonoclasticus

Caputi, Lorenzo; Tullio, Alessandra Di; Leandro, Luana Di; Angelis, Francesco De; Malatesta, Francesco

doi:10.1016/j.bbagen.2005.05.023

Cited by 9 publications

(12 citation statements)

References 43 publications

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“…Recent studies, however, have demonstrated that this approach needs further optimization [10]. Alternatively, modified hemoproteins such as microperoxidases might be used to catalyze hydroxylations by a P450-like oxygen transfer mechanism, but so far these catalysts do not exhibit the necessary performance and selectivity [11][12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Preparation of human drug metabolites using fungal peroxygenases

Poraj-Kobielska

Kinne

Ullrich

et al. 2011

Biochemical Pharmacology

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The synthesis of hydroxylated and O-or N-dealkylated human drug metabolites (HDMs) via selective monooxygenation remains a challenging task for synthetic organic chemists. Here we report that aromatic peroxygenases (APOs; EC 1.11.2.1) secreted by the agaric fungi 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64

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Section: Introductionmentioning

confidence: 99%

Preparation of human drug metabolites using fungal peroxygenases

Poraj-Kobielska

Kinne

Ullrich

et al. 2011

Biochemical Pharmacology

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“…Hydroxylation was favored over peroxidation after addition of ascorbate to the reaction mixture preventing the coupling of phenoxyl radicals [183]. Later, other microperoxidases have been prepared (e.g., MP-9 and MP-11 from horse-heart cytochrome c, MP-5 from cytochrome c 552 of Marinobacter hydrocarbonoclasticus) and they are thought to have a promising potential as a new generation of biocatalysts and/or biomimics in biotechnological applications [182,185,186]. However, to achieve this goal it will be necessary to improve the catalytic properties of MPs, particularly with respect to turnover numbers and enzyme-substrate ratios [184,187].…”

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confidence: 99%

Enzymatic hydroxylation of aromatic compounds

Ullrich

Hofrichter

2007

Cell. Mol. Life Sci.

309

182

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Selective hydroxylation of aromatic compounds is among the most challenging chemical reactions in synthetic chemistry and has gained steadily increasing attention during recent years, particularly because of the use of hydroxylated aromatics as precursors for pharmaceuticals. Biocatalytic oxygen transfer by isolated enzymes or whole microbial cells is an elegant and efficient way to achieve selective hydroxylation. This review gives an overview of the different enzymes and mechanisms used to introduce oxygen atoms into aromatic molecules using either dioxygen (O(2)) or hydrogen peroxide (H(2)O(2)) as oxygen donors or indirect pathways via free radical intermediates. In this context, the article deals with Rieske-type and alpha-keto acid-dependent dioxygenases, as well as different non-heme monooxygenases (di-iron, pterin, and flavin enzymes), tyrosinase, laccase, and hydroxyl radical generating systems. The main emphasis is on the heme-containing enzymes, cytochrome P450 monooxygenases and peroxidases, including novel extracellular heme-thiolate haloperoxidases (peroxygenases), which are functional hybrids of both types of heme-biocatalysts.

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“…[7][8][9][10] Recently, some of us have undertaken a systematic study of an MP from marinobacter hydrocarbonoclasticus, MMP-5 ( Figure 1), to experimentally investigate its electronic properties both in aqueous solution and absorbed over metal substrates. [11,12] From such studies MMP-5 shows rather interesting electronic features which are in line with similar MP. [2] Upon absorption over metal surfaces, the spectroscopic and electric behavior of MMP-5 appears rather different from strictly related systems lacking of peptide side chains.…”

Section: Introductionmentioning

confidence: 84%

“…[12] In aqueous solution, the UV/Vis spectrum results strongly pH-dependent. [11,13] This observation has been explained by considering that the fifth and sixth coordination position of MMP-5 is sensitive to the pH value. At physiological pH values one water molecule and the histidine moiety (His), via its imidazole side chain (see Figure 1), conceivably give rise to a high-spin coordination to the iron porphyrin center.…”

Section: Introductionmentioning

confidence: 91%

“…[17] Such latter geometry has not been considered herein as these calculations require an independent further simulation which will be addressed in forthcoming studies. Note also that the calculations of the free energy associated to the process given in Equation (10) were carried out using Equation (11), implicitly assuming that the average is performed over the statistical ensemble of MMP-5(III). Consequently, our result approximate the actual redox potential as much as the thermodynamic weight of the pentacoordinate complex can be neglected and, also, as much as the statistical ensemble of the oxidized state resembles the statistical ensemble of the reduced state.…”

Section: IImentioning

confidence: 99%

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Conformational and Electronic Properties of a Microperoxidase in Aqueous Solution: A Computational Study

Teodoro¹,

Aschi²,

Amadei³

et al. 2005

ChemPhysChem

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A theoretical study of the conformational properties of a small heme peptide in aqueous solution is carried out by classical, long-timescale molecular dynamics simulations. The electronic properties of this species, that is, the relative energies of its excited electronic states and the redox potential, are reproduced and related to the conformational behavior using the perturbed matrix method and basic statistical mechanics. Our results show an interesting coupling between the conformational transitions and the electronic properties. These investigations, beyond the biophysically relevant results addressing the long-standing question of the actual role of the enzyme structure on the enzyme activity, are also of some methodological interest since they offer a further computational perspective for including the electronic degrees of freedom into the modeling of rather complex molecular systems.

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A new microperoxidase from Marinobacter hydrocarbonoclasticus

Cited by 9 publications

References 43 publications

Preparation of human drug metabolites using fungal peroxygenases

Preparation of human drug metabolites using fungal peroxygenases

Enzymatic hydroxylation of aromatic compounds

Conformational and Electronic Properties of a Microperoxidase in Aqueous Solution: A Computational Study

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