Biological Halogenation has Moved far Beyond Haloperoxidases

Pée, Karl‐Heinz van; Dong, Changjiang; Flecks, Silvana; Naismith, James H.; Patallo, Eugenio P.; Wage, Tobias

doi:10.1016/s0065-2164(06)59005-7

Cited by 61 publications

(46 citation statements)

References 91 publications

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“…Various secondary metabolites of A. aerophoba are found in multiple sponge compartments, raising the possibility that distinct sponge compartments play a role at specific steps of the biosynthetic pathway (45). Interestingly, the haloperoxidase or halogenase enzymes responsible for halogenation processes have only been reported for bacteria, algae, and fungi (3,(81)(82)(83)(84), which suggests that the bacterial endobionts of A. aerophoba could be producing these enzymes (24). Thus, Aplysina sponge cells may produce the inactive precursors of secondary metabolites, while bacteria may provide the enzymes necessary to activate them.…”

Section: Discussionmentioning

confidence: 99%

“…These BAs seem to be located within sponge cells, suggesting a biosynthesis by the sponge (74). However, bromoperoxidase enzymes (responsible for the halogenation reaction that incorporates the bromine into the compound) have only been reported for bacteria, algae, fungi, and plants (3,(81)(82)(83)85). Ebel et al (27) suggest that bacteria may produce the enzymes necessary to transform some of the secondary metabolites in Aplysina aerophoba.…”

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confidence: 99%

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Exploring the Links between Natural Products and Bacterial Assemblages in the SpongeAplysina aerophoba

Sacristán-Soriano

Banaigs

Casamayor

et al. 2011

Appl Environ Microbiol

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The sponge Aplysina aerophoba produces a large diversity of brominated alkaloids (BAs) and hosts a complex microbial assemblage. Although BAs are located within sponge cells, the enzymes that bind halogen elements to organic compounds have been exclusively described in algae, fungi, and bacteria. Bacterial communities within A. aerophoba could therefore be involved in the biosynthesis of these compounds. This study investigates whether changes in both the concentration of BAs and the bacterial assemblages are correlated in A. aerophoba. To do so, we quantified major natural products using high-performance liquid chromatography and analyzed bacterial assemblages using denaturing gradient gel electrophoresis on the 16S rRNA gene. We identified multiple associations between bacteria and natural products, including a strong relationship between a Chloroflexi phylotype and aplysinamisin-1 and between an unidentified bacterium and aerophobin-2 and isofistularin-3. Our results suggest that these bacteria could either be involved in the production of BAs or be directly affected by them. To our knowledge, this is one of the first reports that find a significant correlation between natural products and bacterial populations in any benthic organism. Further investigating these associations will shed light on the organization and functioning of host-endobiont systems such as Aplysina aerophoba.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Exploring the Links between Natural Products and Bacterial Assemblages in the SpongeAplysina aerophoba

Sacristán-Soriano

Banaigs

Casamayor

et al. 2011

Appl Environ Microbiol

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“…120 iodinated, 2100 brominated, 2300 chlorinated, and 30 fluorinated compounds). [13][14][15] Our understanding of biological halogenation also evolved concurrently, and haloperoxidases with various cofactors (heme-containing, vanadium-containing, metal-free, etc.) were discovered.…”

Section: Biological Halogenation and Biomimeticsmentioning

confidence: 99%

“…were discovered. [14,15] The first halogenating agent to be discovered in biological systems was the heme-dependent enzyme chloroperoxidase (isolated from the fungus Caldariomyces fumago) which uses hydrogen peroxide and chloride anions for "electrophilic" chlorination. [16,17] To date, chloroperoxidase from Caldariomyces fumago remains the most studied halogenating enzyme.…”

Section: Biological Halogenation and Biomimeticsmentioning

confidence: 99%

“…Although other routes for halogenation in natural systems have also been discovered, this strategy remains prevalent (excluding fluorination because of the higher oxidation potential of F À ). [15,[28][29][30][31] One especially intriguing question is what is the active halogenating species at the active site of the enzyme? Despite extensive mechanistic studies involving haloperoxidase enzymes, the exact active halogenating intermediate remains unknown.…”

Section: Biological Halogenation and Biomimeticsmentioning

confidence: 99%

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Oxidative Halogenation with “Green” Oxidants: Oxygen and Hydrogen Peroxide

2009

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It is difficult to imagine organic chemistry without organo-halogen compounds and the molecular halogens needed for their preparation. The halogens have very different reactivity, with iodine usually requiring some form of activation, while others are reactive and hazardous chemicals. To avoid their use, various modified reagents have been discovered (N-bromo- and N-chlorosuccinimide, Selectfluor..), but halogens are used to prepare these reagents and when they are used the atom economy is poor. A better approach, which is based on biomimetric research on oxidative halogenation in nature, consists of generating the halogenating reagent in situ under acidic conditions from a halide salt. The result of such a reaction has been halogenation with 100 % halogen atom economy. Suitable oxidants for the oxidation of halides are hydrogen peroxide and oxygen.

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Flavoenzymes, Chemistry of

Berkel

2008

Wiley Encyclopedia of Chemical Biology

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Flavoenzymes are omnipresent in nature and are involved in many cellular processes. Flavoenzymes typically contain the vitamin B2 derivatives FAD and FMN as a redox‐active prosthetic group. By varying the protein environment around the isoalloxazine ring of the flavin, evolution has created a great diversity of flavoprotein active sites and catalytic machineries. Most flavoenzymes perform one‐ or two‐electron redox reactions and belong to the following groups: Flavoprotein reductases primarily use NAD(P)H as electron donor and pass these electrons to a protein substrate or another electron acceptor. Flavoprotein dehydrogenases oxidize organic substrates and mainly use quinones and electron transfer proteins as electron acceptors. Flavoprotein disulfide oxidoreductases contain active‐site thiols. They use a dithiol substrate and NAD + to form a disulfide product and NADH or act in the other direction yielding NAD(P) + and a reduced (dithiol) product. Some flavoprotein (di)thiol oxidoreductases stabilize a reactive and reversibly oxidized cysteine in their active site. Flavoprotein oxidases catalyze the conversion of a substrate single bond to a double bond. The reduced flavin generated during this reaction is reoxidized by molecular oxygen to form hydrogen peroxide. Flavoprotein monooxygenases mainly use NAD(P)H as an electron donor and insert one atom of molecular oxygen into their substrates. By doing so, they act in different biological processes, ranging from lignin degradation and detoxification to the biosynthesis of polyketides and plant hormones.

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Biological Halogenation has Moved far Beyond Haloperoxidases

Cited by 61 publications

References 91 publications

Exploring the Links between Natural Products and Bacterial Assemblages in the SpongeAplysina aerophoba

Exploring the Links between Natural Products and Bacterial Assemblages in the SpongeAplysina aerophoba

Oxidative Halogenation with “Green” Oxidants: Oxygen and Hydrogen Peroxide

Flavoenzymes, Chemistry of

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