Peroxygenases en route to becoming dream catalysts. What are the opportunities and challenges?

Wang, Yonghua; Lan, Dongming; Durrani, Rabia; Hollmann, Frank

doi:10.1016/j.cbpa.2016.10.007

Cited by 216 publications

(202 citation statements)

References 59 publications

Supporting

Mentioning

196

Contrasting

Unclassified

Order By: Relevance

“…Drawbacks of the CYP family are poor (regio-)selectivities, low productivities, uncoupling, and the dependence on NADPH as reducing agent [14,17,18]. The latter may be overcome by P450 peroxygenases, which utilize hydrogen peroxide as oxidant [23]. Additionally, uncoupling is diminished when using peroxygenases since the autoxidation shunt is avoided and H 2 O 2 produced by the peroxide shunt can be used in the next cycle (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…BM3 from Bacillus megaterium, CYP102A1) are rendered self-sufficient by being fused to the reductase domain and are described as class VIII P450 enzymes [49]. Other P450s are categorized as peroxygenases due to their ability to utilize hydrogen peroxide (H 2 O 2 ) as both, electron-and oxygen-source [23]. Regarding (synthetic) applicability, self-sufficient CYPs or peroxygenases possess the advantage of simplifying the reaction system, as no additional enzyme for electron transfer is required.…”

Section: Cytochrome P450 Classesmentioning

confidence: 99%

“…H 2 O 2 ) to the substrate. Fatty acids (C12:0 to C20:0) are hydroxylated close to the terminus and subsequent overoxidation yields subterminal ketones or dicarboxylic acids [21][22][23]. 12-Hydroxylases (EC 1.14.13.26) display remarkable regioselectivity as they convert oleic acid to ricinoleic acid via hydroxylation exclusively at the C-12 position in homoallylic position to the C=C double bond [24].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Cytochrome P450 Classesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

View full text Add to dashboard Cite

show abstract

“…Although a yeast expression system for AaeUPO has been developed after enzyme directed evolution, 33 new procedures and hosts for expressing wild-type genes of this and other UPOs are required for investigating active-site residues and engineering UPO biocatalysts for selective oxygenation reactions of biotechnological interest. 34 …”

Section: View Article Onlinementioning

confidence: 99%

Selective synthesis of the resveratrol analogue 4,4′-dihydroxy-trans-stilbene and stilbenoids modification by fungal peroxygenases

Aranda

Ullrich

Kiebist

et al. 2018

Catal. Sci. Technol.

View full text Add to dashboard Cite

aThis work gives first evidence that the unspecific peroxygenases (UPOs) from the basidiomycetes Agrocybe aegerita (AaeUPO), Coprinopsis cinerea (rCciUPO) and Marasmius rotula (MroUPO) are able to catalyze the regioselective hydroxylation of trans-stilbene to 4,4′-dihydroxy-trans-stilbene (DHS), a resveratrol (RSV) analogue whose preventive effects on cancer invasion and metastasis have very recently been shown. Nearly complete transformation of substrate (yielding DHS) was achieved with the three enzymes tested, using H 2 O 2 as the only co-substrate, with AaeUPO showing exceptionally higher total turnover number (200 000) than MroUPO (26 000) and rCciUPO (1400). Kinetic studies demonstrated that AaeUPO was the most efficient enzyme catalyzing stilbene dihydroxylation with catalytic efficiencies (k cat /K m ) one and two orders of magnitude higher than those of MroUPO and rCciUPO, so that 4-hydroxystilbene appears to be the best UPO substrate reported to date. In contrast, the peroxygenase from the ascomycete Chaetomium globosum (CglUPO) failed to hydroxylate trans-stilbene at the aromatic ring and instead produced the trans-epoxide in the alkenyl moiety. In addition, stilbenoids such as pinosylvin (Pin) and RSV were tested as substrates for the enzymatic synthesis of RSV from Pin and oxyresveratrol (oxyRSV) from both RSV and Pin. Overall, lower conversion rates and regioselectivities compared with trans-stilbene were accomplished by three of the UPOs, and no conversion was observed with CglUPO. The highest amount of RSV (63% of products) and oxyRSV (78%) were again attained with AaeUPO. True peroxygenase activity was demonstrated by incorporation of 18 O from H 2 18O 2 into the stilbene hydroxylation products. Differences in the number of phenylalanine residues at the heme access channels seems related to differences in aromatic hydroxylation activity, since they would facilitate substrate positioning by aromatic-aromatic interactions. The only ascomycete UPO tested (that of C. globosum) turned out to have the most differing active site (distal side of heme cavity) and reactivity with stilbenes resulting in ethenyl epoxidation instead of aromatic hydroxylation. The above oxyfunctionalizations by fungal UPOs represent a novel and simple alternative to chemical synthesis for the production of DHS, RSV and oxyRSV.

show abstract

“…[151] This cascade uses four heterologously expressed recombinant enzymes with cofactors provided by the host cell and isopropyl amine as the amine donor.T he initial CÀHactivation is performed by aCYP monooxygenase (Y96F) and results in the non-stereoselective hydroxylation of the benzylic position. [153] The synthetic viability was recently shown by Hollmann et al, combining photocatalytic H 2 O 2 generation from H 2 Owith an anatase-Au-TiO 2 photocatalyst with rAaeUPO peroxygenase-catalyzed stereoselective hydroxylation of ethylbenzene (Scheme 34). In the second step,t wo alcohol dehydrogenases with complementary stereoselectivity are employed.…”

Section: Reviewsmentioning

confidence: 99%

Catalytic Aerobic Oxidation of C(sp³)−H Bonds

2019

View full text Add to dashboard Cite

Oxidation reactions are a key technology to transform hydrocarbons from petroleum feedstock into chemicals of a higher oxidation state, allowing further chemical transformations. These bulk scale oxidation processes usually employ molecular oxygen as the terminal oxidant as at this scale it is typically the only economically viable oxidant. The produced commodity chemicals possess limited functionality and usually show a high degree of symmetry thereby avoiding selectivity issues. In sharp contrast in the production of fine chemicals preference is still given to classical oxidants. Considering the strive for greener production processes the use of O2, the most abundant and greenest oxidant, is a logical choice. Given the rich functionality and complexity of fine chemicals achieving regio/chemoselectivity is a major challenge. This review presents an overview of the most important catalytic systems recently described for aerobic oxidation, and the current insight in their reaction mechanism.

show abstract

Peroxygenases en route to becoming dream catalysts. What are the opportunities and challenges?

Cited by 216 publications

References 59 publications

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Selective synthesis of the resveratrol analogue 4,4′-dihydroxy-trans-stilbene and stilbenoids modification by fungal peroxygenases

Catalytic Aerobic Oxidation of C(sp³)−H Bonds

Contact Info

Product

Resources

About

Peroxygenases en route to becoming dream catalysts. What are the opportunities and challenges?

Cited by 216 publications

References 59 publications

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Selective synthesis of the resveratrol analogue 4,4′-dihydroxy-trans-stilbene and stilbenoids modification by fungal peroxygenases

Catalytic Aerobic Oxidation of C(sp3)−H Bonds

Contact Info

Product

Resources

About

Catalytic Aerobic Oxidation of C(sp³)−H Bonds