Parameters for bromination of pyrroles in bromoperoxidase-catalyzed oxidations

Wischang, Diana; Hartung, Jens

doi:10.1016/j.tet.2011.04.010

Cited by 34 publications

(20 citation statements)

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“…In the brown alga A. nodosum, the two VBPO isoenzymes present at different locations in the alga [61,71] feature distinct biochemical and structural properties [60], suggesting distinct biological roles in the algal physiology. In vitro halogenation experiments have shown that purified native VBPOI from A. nodosum catalyzes the bromination of pyrroles [72] or phenols [73], whereas the second VBPO is involved in the biosynthesis of methyl 4-bromopyrrole-2-carboxylate, a natural product isolated from the marine sponge [60]. Laminaria digitata also features two isoforms of VHPOs, but with distinct halide specificities.…”

Section: Vanadium Haloperoxidase -Catalyzed Halogenationmentioning

confidence: 99%

“…However, recent studies [56] have shown that the influence of the protein stabilization of the active center goes beyond the first coordination sphere. At the long term, the biochemical and structural characterizations of known and supplementary VHPOs will be necessary, in particular at very high resolution (beyond 1 Å) and possibly using neutron-diffraction to precisely locate proton M a n u s c r i p t 31 3-bromo-8-epicaparrapi oxide [80], bromofuranone [80], napyradiomycin [68], merochlorin [69,70], bromopyrroles [72] and bromophenols [73]. …”

Section: Outlook: Merging Xanes and Exafsmentioning

confidence: 99%

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Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Leblanc

Vilter

Fournier

et al. 2015

Coordination Chemistry Reviews

128

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In the environment, vanadium-dependent haloperoxidases (VHPO) are likely to play a key role in the production of biogenic organo-halogens. These enzymes contain vanadate as a prosthetic group, and catalyze, in the presence of hydrogen peroxide, the oxidation of halide ions (Cl -, Br -or I -). They are classified according to the most electronegative halide that they can oxidize. Since the first discovery of a vanadium bromoperoxidase in the brown alga Ascophyllum nodosum thirty years ago, structural and mechanistic studies have been mainly conducted on two types of VHPO, chloro-and bromoperoxidases, and more recently on a vanadium-dependent iodoperoxidase. In this review, we highlight the main progress obtained on the structure-function relation of these proteins, based on biochemistry, crystallography and X-ray absorption spectroscopy (XAS). The comparison of 3D protein structures of the different VHPO helped identify the residues that govern the molecular mechanisms of catalysis and specificity of VHPO. Vanadium K-edge XAS gave further important insight to understand the fine changes around the vanadium cofactor during the catalytic cycle. The combination of different structural approaches, at different scales of resolution, shed new light on biological vanadium coordination in the active site, and its importance for the catalytic cycle and halide specificity of vanadium haloperoxidases. Keywords (max 6)Vanadium-dependent haloperoxidase, vanadium coordination, crystallographic structure, structural evolution, oligomeric state, X-ray absorption spectroscopy on biological vanadium

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Section: Vanadium Haloperoxidase -Catalyzed Halogenationmentioning

confidence: 99%

Section: Outlook: Merging Xanes and Exafsmentioning

confidence: 99%

Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Leblanc

Vilter

Fournier

et al. 2015

Coordination Chemistry Reviews

128

View full text Add to dashboard Cite

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“…CoVBPO [24] 1.00 0.06 ---470 (Br) rCoVBPO [25] 1.20 0.02 1.80---CpVBPO [11c] 11.0 0.09 ---26.3 (Br) browna lgae AnIVBPO [18,26] 3.70 0.06 0.20 [b] 344 85 127 (Br) 2 10 4 0.49 (Cl) fungi…”

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confidence: 99%

Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential

et al. 2016

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Vanadium-dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium Acaryochloris marina (AmVHPO), including its structure determination by X-ray crystallography. Compared to other VHPOs, the AmVHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high-yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.

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“…Despite the hazardous nature of liquid molecular bromine, it is used for the production of a large fraction of industrial and chemical organobromine compounds. [17] Molecular bromine is a toxic, volatile and corrosive chemical that restricts its use as a brominating agent. Whereas, the formation of in situ bromine from the oxidation of bromide by oxygen or hydrogen peroxide is much more economical and green.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and characterization of dimeric μ‐oxidovanadium complexes as the functional model of vanadium bromoperoxidase

Maurya

Mahato

Chaudhary

et al. 2020

Applied Organom Chemis

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Two vanadium (IV) complexes [VIVO(Haeae‐sal)(MeOH)]+ (1) and [VIVO(Haeae‐hyap)(MeOH)]+ (2) were prepared by reacting [VO(acac)2] with ligands [H2aeae‐sal] (I) and [H2aeae‐hyap] (II) respectively. Condensation of 2‐(2‐aminoethylamino)ethanol with salicylaldehyde and 2‐hydroxyacetophenone produces the ligands (I) and (II) respectively. Both vanadium complexes 1 and 2 are sensitive towards aerial oxygen in solution and rapidly convert into vanadium(V) dioxido species. Vanadium(V) dioxido species crystalizes as the dimeric form in the solid‐state. Single‐crystal XRD analysis suggests octahedral geometry around each vanadium center in the solid‐state. To access the benefits of heterogeneous catalysis, vanadium(V) dioxido complexes were anchored into the polymeric chain of chloromethylated polystyrene. All the synthesized neat and supported vanadium complexes have been studied by a number of techniques to confirm their structural and functional properties. Bromoperoxidase activity of the synthesized vanadium(V) dioxido complexes 3 and 4 was examined by carrying out oxidative bromination of salicylaldehyde and oxidation of thioanisole. In the presence of hydrogen peroxide, 3 shows 94.4% conversion (TOF value of 2.739 × 102 h−1) and 4 exhibits 79.0% conversion (TOF value of 2.403 × 102 h−1) for the oxidative bromination of salicylaldehyde where 5‐bromosalicylaldehyde appears as the major product. Catalysts 3 and 4 also efficiently catalyze the oxidation of thioanisole in the presence of hydrogen peroxide where sulfoxide is observed as the major product. Covalent attachment of neat catalysts 3 and 4 into the polymer chain enhances substrate conversion (%) and their catalytic efficiency increases many folds, both in the oxidative bromination and oxidation of thioether. Polymer supported catalysts 5 displayed 98.8% conversion with a TOF value of 1.127 × 104 h−1 whereas catalyst 6 showed 95.7% conversion with a TOF value of 4.675 × 103 h−1 for the oxidative bromination of salicylaldehyde. These TOF values are the highest among the supported vanadium catalysts available in the literature for the oxidative bromination of salicylaldehyde.

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Parameters for bromination of pyrroles in bromoperoxidase-catalyzed oxidations

Cited by 34 publications

References 50 publications

Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential

Synthesis and characterization of dimeric μ‐oxidovanadium complexes as the functional model of vanadium bromoperoxidase

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