Biocatalytic production of 5-hydroxy-2-adamantanone by P450cam coupled with NADH regeneration

Furuya, Toshiki; Kanno, Takaaki; Yamamoto, Hiroaki; Kimoto, Norihiro; Matsuyama, Akinobu; Kino, Kuniki

doi:10.1016/j.molcatb.2013.05.003

Cited by 5 publications

(6 citation statements)

References 36 publications

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“…CYP101B1 oxidation of 2‐adamantanone, 4 , generated two products (both m/z =166.1, Figure S3(a)) and these were synthesised using a whole‐cell oxidation system . After separation by silica gel chromatography the hydroxylated metabolites were identified by their mass fragmentation pattern and NMR spectra as 6‐hydroxy‐2‐adamantanone, 4 a (55 %) and 5‐hydroxy‐2‐adamantanone, 4 b (45 %, Scheme , Figure S3(a), Figure S4, Figure S5(a), Figure S5(b)) …”

Section: Resultsmentioning

confidence: 99%

“…Microbial oxidative biotransformations of adamantane, 1 , 2‐adamantanone, 4 , adamantanols, 2 and 3 , and related substrates including the acetate esters are possible using different bacteria, including Streptomyces, and fungi including Basidiomycota , Absidia cylindrospora and Beauveria (Sporotrichum ) sulfurescens . Certain P450 enzymes and their mutants have also been reported to oxidise adamantane based substrates including CYP101 A1 and CYP101D2 though at lower activities than the turnover of the esters reported here …”

Section: Discussionmentioning

confidence: 99%

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The Use of Directing Groups Enables the Selective and Efficient Biocatalytic Oxidation of Unactivated Adamantyl C‐H Bonds

et al. 2016

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Adamantane, 1‐ and 2‐adamantanol and 2‐adamantanone, were poor substrates for the cytochrome P450 enzyme CYP101B1. The CYP101B1 catalysed oxidation of 1‐adamantyl methyl ketone, and methyl 2‐(1‐adamantyl acetate), were more active generating a majority of the 4‐hydroxy metabolite. Substrate engineering using acetate and isobutyrate ester directing groups significantly increased the affinity, activity and coupling efficiency of CYP101B1 for the esters compared to the parent adamantanols, resulting in enhanced product formation rates (720 to 1350 nmol.(nmol‐P450)−1.min−1). The majority of the turnovers were selective for C−H bond hydroxylation with 4‐hydroxy‐1‐adamantyl isobutyrate and the 5‐hydroxy‐2‐adamantyl esters being generated as the sole majority product, 97 %, with high total turnover numbers, ranging from 4130 to 16500. In addition N‐(1‐adamantyl)acetamide, was oxidised by CYP101B1 whereas 1‐adamantylamine, was not. Whole‐cell biocatalytic reactions were used to generate the products in good yield. Overall the use of ester protecting groups and the modification of the amine to an amide enabled the more efficient and selective biocatalytic oxidation of adamantane frameworks.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The Use of Directing Groups Enables the Selective and Efficient Biocatalytic Oxidation of Unactivated Adamantyl C‐H Bonds

et al. 2016

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“…GC–MS analysis was performed using a 6890 system (Agilent, Palo Alto, CA, USA) equipped with a DB-5 ms column (0.32 × 30 mm, Agilent) 41 , 42 . The post-reaction mixture was acidified by the addition of HCl (pH 2–3), and ethyl acetate (1 mL) was then added.…”

Section: Methodsmentioning

confidence: 99%

Isolation and characterization of microorganisms capable of cleaving the ether bond of 2-phenoxyacetophenone

Oya

Tonegawa

Nakagawa

et al. 2022

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Lignin is a heterogeneous aromatic polymer and major component of plant cell walls. The β-O-4 alkyl aryl ether is the most abundant linkage within lignin. Given that lignin is effectively degraded on earth, as yet unknown ether bond–cleaving microorganisms could still exist in nature. In this study, we searched for microorganisms that transform 2-phenoxyacetophenone (2-PAP), a model compound for the β-O-4 linkage in lignin, by monitoring ether bond cleavage. We first isolated microorganisms that grew on medium including humic acid (soil-derived organic compound) as a carbon source. The isolated microorganisms were subsequently subjected to colorimetric assay for 2-PAP ether bond–cleaving activity; cells of the isolated strains were incubated with 2-PAP, and strains producing phenol via ether bond cleavage were selected using phenol-sensitive Gibbs reagent. This screening procedure enabled the isolation of various 2-PAP–transforming microorganisms, including 7 bacteria (genera: Acinetobacter, Cupriavidus, Nocardioides, or Streptomyces) and 1 fungus (genus: Penicillium). To our knowledge, these are the first microorganisms demonstrated to cleave the ether bond of 2-PAP. One Gram-negative bacterium, Acinetobacter sp. TUS-SO1, was characterized in detail. HPLC and GC–MS analyses revealed that strain TUS-SO1 oxidatively and selectively cleaves the ether bond of 2-PAP to produce phenol and benzoate. These results indicate that the transformation mechanism differs from that involved in reductive β-etherase, which has been well studied. Furthermore, strain TUS-SO1 efficiently transformed 2-PAP; glucose-grown TUS-SO1 cells converted 1 mM 2-PAP within only 12 h. These microorganisms might play important roles in the degradation of lignin-related compounds in nature.

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“…However, because P450 monooxygenases require NAD(P)H as a coenzyme, this biotechnological process can be complicated as a continuous supply of this expensive coenzyme is required for P450s to achieve high-yield production of oxidized chemicals. 9 , 10 In contrast, P450 peroxygenases utilize hydrogen peroxide (H 2 O 2 ) instead of O 2 to generate compound I. Because P450 peroxygenases do not require NAD(P)H, these enzymes are advantageous for practical applications.…”

Section: Introductionmentioning

confidence: 99%

Sustainable Approach for Peroxygenase-Catalyzed Oxidation Reactions Using Hydrogen Peroxide Generated from Spent Coffee Grounds and Tea Leaf Residues

et al. 2022

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Peroxygenases are promising catalysts for use in the oxidation of chemicals as they catalyze the direct oxidation of a variety of compounds under ambient conditions using hydrogen peroxide (H 2 O 2 ) as an oxidant. Although the use of peroxygenases provides a simple method for oxidation of chemicals, the anthraquinone process currently used to produce H 2 O 2 requires significant energy input and generates considerable waste, which negatively affects process sustainability and production costs. Thus, generating H 2 O 2 for peroxygenases on site using an environmentally benign method would be advantageous. Here, we utilized spent coffee grounds (SCGs) and tea leaf residues (TLRs) for the production of H 2 O 2 . These waste biomass products reacted with molecular oxygen and effectively generated H 2 O 2 in sodium phosphate buffer. The resulting H 2 O 2 was utilized by the bacterial P450 peroxygenase, CYP152A1. Both SCG-derived and TLR-derived H 2 O 2 promoted the CYP152A1-catalyzed oxidation of 4-methoxy-1-naphthol to Russig’s blue as a model reaction. In addition, when CYP152A1 was incubated with styrene, the SCG and TLR solutions enabled the synthesis of styrene oxide and phenylacetaldehyde. This new approach using waste biomass provides a simple, cost-effective, and sustainable oxidation method that should be readily applicable to other peroxygenases for the synthesis of a variety of valuable chemicals.

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Biocatalytic production of 5-hydroxy-2-adamantanone by P450cam coupled with NADH regeneration

Cited by 5 publications

References 36 publications

The Use of Directing Groups Enables the Selective and Efficient Biocatalytic Oxidation of Unactivated Adamantyl C‐H Bonds

The Use of Directing Groups Enables the Selective and Efficient Biocatalytic Oxidation of Unactivated Adamantyl C‐H Bonds

Isolation and characterization of microorganisms capable of cleaving the ether bond of 2-phenoxyacetophenone

Sustainable Approach for Peroxygenase-Catalyzed Oxidation Reactions Using Hydrogen Peroxide Generated from Spent Coffee Grounds and Tea Leaf Residues

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