103618-27-5Relevant articles and documents
Synthesis of (+/-)-Desmarestene and (+/-)-Viridiene, the Two Sperm Releasing and Attracting Pheromones from the Brown Algae Desmarestia aculeata and Desmarestia viridis
Boland, Wilhelm,Jakoby, Karin,Jaenicke, Lothar
, p. 2355 - 2362 (1982)
Desmarestene 1 6-(1Z,3-butadienyl)-1,4-cycloheptadiene) and viridiene 3 cis-3-(1Z,3-butadienyl)-4-vinylcyclopentene) are chemical messengers for male gametes of the brown algae Desmarestia aculeata and Desmarestia viridis.Total syntheses of 1, 3 and their stereoisomers 1a, 3a-c are reported.Gas-chromatographic comparison of synthetic 1 and 3 with the corresponding natural products has established their structural identity.
Resolution of fused bicyclic ketones by a recombinant biocatalyst expressing the Baeyer-Villiger monooxygenase gene Rv3049c from Mycobacterium tuberculosis H37Rv
Snajdrova, Radka,Grogan, Gideon,Mihovilovic, Marko D.
, p. 4813 - 4817 (2006)
Recombinant Escherichia coli B834 (DE3) pDB5 expressing the Rv3049c gene encoding a Baeyer-Villiger monooxygenase from Mycobacterium tuberculosis H37Rv was used for regioselective oxidations of fused bicyclic ketones. This whole-cell system represents the first recombinant Baeyer-Villiger oxidation biocatalyst that effectively resolves the racemic starting materials in this series. Within biotransformations using this organism one substrate enantiomer remains in high optical purity, while the second enantiomer is oxidized to one type of regioisomeric lactone preferably.
Divorce in the two-component BVMO family: The single oxygenase for enantioselective chemo-enzymatic Baeyer-Villiger oxidations
R?llig, Robert,Paul, Caroline E.,Claeys-Bruno, Magalie,Duquesne, Katia,Kara, Selin,Alphand, Véronique
, p. 3441 - 3450 (2021)
Two-component flavoprotein monooxygenases consist of a reductase and an oxygenase enzyme. The proof of functionality of the latter without its counterpart as well as the mechanism of flavin transfer remains unanswered beyond doubt. To tackle this question, we utilized a reductase-free reaction system applying purified 2,5-diketocamphane-monooxygenase I (2,5-DKCMO), a FMN-dependent type II Baeyer-Villiger monooxygenase, and synthetic nicotinamide analogues (NCBs) as dihydropyridine derivatives for FMN reduction. This system demonstrated the stand-alone quality of the oxygenase, as well as the mechanism of FMNH2transport by free diffusion. The efficiency of this reductase-free system strongly relies on the balance of FMN reduction and enzymatic (re)oxidation, since reduced FMN in solution causes undesired side reactions, such as hydrogen peroxide formation. Design of experiments allowed us to (i) investigate the effect of various reaction parameters, underlining the importance to balance the FMN/FMNH2cycle, (ii) optimize the reaction system for the enzymatic Baeyer-Villiger oxidation of rac-bicyclo[3.2.0]hept-2-en-6-one,rac-camphor, andrac-norcamphor. Finally, this study not only demonstrates the reductase-independence of 2,5-DKCMO, but also revisits the terminology of two-component flavoprotein monooxygenases for this specific case.
Discovery of Baeyer-Villiger monooxygenases from photosynthetic eukaryotes
Beneventi, Elisa,Niero, Mattia,Motterle, Riccardo,Fraaije, Marco,Bergantino, Elisabetta
, p. 145 - 154 (2013)
Baeyer-Villiger monooxygenases are attractive "green" catalysts able to produce chiral esters or lactones starting from ketones. They can act as natural equivalents of peroxyacids that are the catalysts classically used in the organic synthesis reactions, consisting in the cleavage of CC bonds with the concomitant insertion of an oxygen atom. In this study, two type I BVMOs have been identified for the first time in photosynthetic eukaryotic organisms, the red alga Cyanidioschyzon merolae (Cm) and the moss Physcomitrella patens (Pp). A biocatalytic characterization of these newly discovered enzymes, expressed in recombinant forms, was carried out. Both enzymes could be purified as holo enzymes containing a FAD cofactor. Their thermostability was investigated and revealed that the Cm-BVMO is the most thermostable type I BVMO with an apparent melting temperature of 56 C. Substrate profiling revealed that both eukaryotic BVMOs accept a wide range of ketones which include aromatic, aliphatic, aryl aliphatic and bicyclic ketones. In particular, linear aliphatic ketones (C9 and C12), carrying the keto functionality in different positions, resulted to be the best substrates in steady state kinetic analyses. In order to restore the BVMO-typifying sequence motif in the Pp-BVMO, a mutant was prepared (Y160H). Intriguingly, this mutation resulted in higher activities on most tested substrates. The recombinant enzymes displayed kcat values in the 0.1-0.2 s-1 range, which is relatively low when compared with other known type I BVMOs. This may hint to a role in secondary metabolism in these photosynthetic organisms, though their exact function remains to be established.
Controlling the Regioselectivity of Baeyer–Villiger Monooxygenases by Mutation of Active-Site Residues
Balke, Kathleen,B?umgen, Marcus,Bornscheuer, Uwe T.
, p. 1627 - 1638 (2017)
Baeyer–Villiger monooxygenase (BVMO)-mediated regiodivergent conversions of asymmetric ketones can lead to the formation of “normal” or “abnormal” lactones. In a previous study, we were able to change the regioselectivity of a BVMO by mutation of the active-site residues to smaller amino acids, which thus created more space. In this study, we demonstrate that this method can also be used for other BVMO/substrate combinations. We investigated the regioselectivity of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase from Pseudomonas putida (OTEMO) for cis-bicyclo[3.2.0]hept-2-en-6-one (1) and trans-dihydrocarvone (2), and we were able to switch the regioselectivity of this enzyme for one of the substrate enantiomers. The OTEMO wild-type enzyme converted (?)-1 into an equal (50:50) mixture of the normal and abnormal products. The F255A/F443V variant produced 90 % of the normal product, whereas the W501V variant formed up to 98 % of the abnormal product. OTEMO F255A exclusively produced the normal lactone from (+)-2, whereas the wild-type enzyme was selective for the production of the abnormal product. The positions of these amino acids were equivalent to those mutated in the cyclohexanone monooxygenases from Arthrobacter sp. and Acinetobacter sp. (CHMOArthro and CHMOAcineto) to switch their regioselectivity towards (+)-2, which suggests that there are hot spots in the active site of BVMOs that can be targeted with the aim to change the regioselectivity.
Asymmetric baeyer-villiger oxidation of 2,3- and 2,3,4-substituted cyclobutanones catalyzed by chiral phosphoric acids with aqueous H 2O2 as the oxidant
Xu, Senmiao,Wang, Zheng,Zhang, Xumu,Ding, Kuiling
, p. 110 - 116 (2011)
Catalytic asymmetric Baeyer-Villiger (B-V) oxidation of 2,3,4-trisubstituted cyclobutanone (4) has been realized by the catalysis of a 1,1′-bi-2-naphthol (BINOL)-derived chiral phosphoric acid (1j), which contains bulky 2,4,6-triisopropyl phenyl groups at the 3,3′-positions of the BINOL backbone, using 30% aqueous H2O2 as the oxidant, affording the corresponding Iγ-lactone (5) in 99% yield with 95% ee. In a divergent kinetic resolution of racemic 2,3-disubstituted bicyclic cyclobutanones (6) through asymmetric B-V oxidation, the chiral phosphoric acid 1p demonstrated excellent catalytic performance, giving a range of regioisomeric chiral lactones in a normal lactone (nl)/abnormal lactone (al) ratio of up to 2.1:1, with up to 99% ee in the al product. It was found that fine tuning of the stereoelectronic properties of the backbone in chiral phosphoric acids is critically important for attaining high levels of enantioselectivity in the catalysis of B-V reactions of different type of cyclobutanones. The present work has provided a convenient approach to the synthesis of a variety of optically active chiral Iγ-lactones. Asymmetric Baeyer-Villiger oxidation of tricyclic cyclobutaone and a variety of racemic bicyclic cyclobutanone derivatives has been realized by the catalysis of 1,1′-bi-2-naphthol (BINOL)-derived chiral phosphoric acid with high yields and excellent enantioselectivities using 30% aqueous H2O2 as the oxidant.
A short chemoenzymatic synthesis of (+)-Multifidene and (+)-Viridiene
Lebreton, Jacques,Alphand, Veronique,Furstoss, Roland
, p. 1011 - 1014 (1996)
(+)-Multifidene 1 and (+)-Viridiene 2, the major constituents of some brown algae pheromones, were synthesized in five steps from racemic bicycloheptenone 3 via a novel microbiological Baeyer-Villiger oxidation performed using the fungi Cunninghamella echinulata.
Greener Preparation of 5-Ethyl-4a-hydroxyisoalloxazine and Its Use for Catalytic Aerobic Oxygenations
Oonishi, Takahiro,Kawahara, Takayuki,Arakawa, Yukihiro,Minagawa, Keiji,Imada, Yasushi
, p. 1791 - 1795 (2019)
Isoalloxazine ring systems are found in flavin cofactors in nature, and the simulation of their redox catalyses is an important task for developing sustainable catalytic oxidation reactions. Although 5-ethyl-4a-hydroxyisoalloxazines are among the most promising candidates as catalyst for such purposes, the use of them for laboratorial as well as industrial synthetic chemistry has so far been quite limited presumably due to the lack of their preparation methods readily, safely, and inexpensively available. In this communication, we introduce an environmentally benign and practical preparation of 5-ethyl-4a-hydroxy-3,7,8,10-tetramethylisoalloxazine (1EtOH) from 3,7,8,10-tetramethylisoalloxazine (1), in which conventional synthetic requirements, including (i) operations under inert conditions, (ii) risky or expensive chemicals, and (iii) isolation of labile intermediates, have all been dissolved. In addition, we have presented that 1EtOH could be an effective catalyst for Baeyer–Villiger oxidation as well as sulfoxidation with molecular oxygen (O2) as a terminal oxidant under suitable conditions, which is the first report on aerobic oxygenations catalyzed by 5-alkyl-4a-hydroxyisoalloxazines.
Alloxazinium-Resins as Readily Available and Reusable Oxidation Catalysts
Arakawa, Yukihiro,Imada, Yasushi,Kawahara, Takayuki,Minagawa, Keiji
supporting information, p. 1728 - 1730 (2021/07/19)
N5-Modified alloxazinium salts including 5-ethyl-1,3-dimethylalloxazinium and 5-ethyl-1,3-dimethyl-8-(trifluoromethyl)- A lloxazinium salts were readily prepared as alloxazinium-resins from the corresponding N5-unmodified ingredients via the aerobic oxidationion exchange protocol, previously introduced by us for the preparation of isoalloxazine analogues, and their catalysis and reusability in H2O2 oxidations were evaluated.
