Construction of a whole-cell biohybrid catalyst using a Cp*Rh(III)-dithiophosphate complex as a precursor of a metal cofactor

Kato, S.; Onoda, Akira; Grimm, Alexander R.; Schwaneberg, Ulrich; Hayashi, Takashi

doi:10.1016/j.jinorgbio.2020.111352

Cited by 12 publications

(12 citation statements)

References 39 publications

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“…1 H NMR, 13 C NMR, and 19 F NMR spectra were recorded using Bruker Avance 600 or 400 MHz spectrometers. All the NMR experiments were carried out at 298 K. 2D spectra (double-quantum filtered correlation spectroscopy (DQF-COSY), 1 H− 13 C heteronuclear single-quantum coherence (HSQC) spectroscopy, and 1 H− 13 C heteronuclear multiple bond correlation (HMBC) spectroscopy) were acquired with standard pulse sequences using a Bruker Avance 600 MHz equipped with a triple resonance cryoprobe.…”

Section: Acs Catalysismentioning

confidence: 99%

“…All the NMR experiments were carried out at 298 K. 2D spectra (double-quantum filtered correlation spectroscopy (DQF-COSY), 1 H− 13 C heteronuclear single-quantum coherence (HSQC) spectroscopy, and 1 H− 13 C heteronuclear multiple bond correlation (HMBC) spectroscopy) were acquired with standard pulse sequences using a Bruker Avance 600 MHz equipped with a triple resonance cryoprobe. 1D 13 C and 19 F spectra were recorded using a Bruker Avance 400 MHz. All the spectra were processed with Topspin 2.1 (Bruker).…”

Section: Acs Catalysismentioning

confidence: 99%

“…The data matrix was zero-filled in both dimensions to give a matrix of 4096 × 2048 points and was resolution-enhanced in both dimensions using a cosine bell function before Fourier transformation. The 1 H− 13 C HSQC and 1 H− 13 C HMBC experiments were performed in the 1 H detection mode by single-quantum coherence with proton decoupling in the 13 C domain using data sets of 2048 × 400 points. The 1 H− 13 C HSQC experiment was performed using sensitivity improvement, and in the phase-sensitive mode using echo/antiecho gradient selection, with multiplicity editing during the selection step, 56 setting the one-bond heteronuclear coupling value to 145 Hz.…”

Section: Acs Catalysismentioning

confidence: 99%

“…The 1 H− 13 C HSQC experiment was performed using sensitivity improvement, and in the phase-sensitive mode using echo/antiecho gradient selection, with multiplicity editing during the selection step, 56 setting the one-bond heteronuclear coupling value to 145 Hz. The 1 H− 13 C HMBC experiment was optimized on long-range coupling constants, with a low-pass J filter to suppress onebond correlations, using gradient pulses for selection. The data matrix in all the heteronuclear experiments was extended to 2048 × 1024 points using a forward linear prediction.…”

Section: Acs Catalysismentioning

confidence: 99%

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Highly Selective Indole Oxidation Catalyzed by a Mn-Containing Artificial Mini-Enzyme

et al. 2021

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Indole oxidation represents a real challenge for selectivity because it typically leads to complex mixtures of products even when highly selective enzymes are used. Here, we describe the catalytic potential of an artificial enzyme, Mn-Mimochrome VI*a (Mn-MC6*a), in promoting indole oxidation. This mini-enzyme contains a manganese−deuteroporphyrin active site within a scaffold of two synthetic small peptides covalently linked to porphyrin. Mn-MC6*a promotes the selective oxidation of indole at its C3 position, leading to a 3-oxindole derivative (2-TFE-3oxindole) with unprecedented product selectivity (86% at pH 8.5) compared to native or artificial heme-enzymes. We also suggest a possible reaction mechanism based on the effect of pH, cosolvent, and indole substitution on the reaction outcome. These studies demonstrate that Mn-MC6*a is an excellent artificial peroxygenase for the production of 3-oxindole-containing compounds as key building blocks for the synthesis of fine chemicals.

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Section: Acs Catalysismentioning

confidence: 99%

Section: Acs Catalysismentioning

confidence: 99%

Section: Acs Catalysismentioning

confidence: 99%

Section: Acs Catalysismentioning

confidence: 99%

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Highly Selective Indole Oxidation Catalyzed by a Mn-Containing Artificial Mini-Enzyme

et al. 2021

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“…Due to the protection of cell walls and membranes, whole-cell biocatalysts can be applied in harsh conditions and unconventional reaction systems, 12,13 and the cost is only one-tenth of a puried enzyme system. 10 In addition, whole-cell biocatalysts are commonly used when cofactors are involved in the reaction, 14 such as the reactions catalyzed by oxidoreductases that depend on nicotinamide cofactors 15,16 and the redox-neutral multi-step reactions coupling of enzymes. 17,18 Undeniably, whole-cell biocatalysts have limitations.…”

Section: Introductionmentioning

confidence: 99%

Improving the catalytic performance of Pichia pastoris whole-cell biocatalysts by fermentation process

et al. 2021

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Design of Artificial Enzymes: Insights into Protein Scaffolds

2023

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The design of artificial enzymes has emerged as a promising tool for the generation of potent biocatalysts able to promote new-to-nature reactions with improved catalytic performances, providing a powerful platform for wide-ranging applications and a better understanding of protein functions and structures. The selection of an appropriate protein scaffold plays a key role in the design process. This review aims to give a general overview of the most common protein scaffolds that can be exploited for the generation of artificial enzymes. Several examples are discussed and categorized according to the strategy used for the design of the artificial biocatalyst, namely the functionalization of natural enzymes, the creation of a new catalytic site in a protein scaffold bearing a wide hydrophobic pocket and de novo protein design. The review is concluded by a comparison of these different methods and by our perspective on the topic.

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Construction of a whole-cell biohybrid catalyst using a Cp*Rh(III)-dithiophosphate complex as a precursor of a metal cofactor

Cited by 12 publications

References 39 publications

Highly Selective Indole Oxidation Catalyzed by a Mn-Containing Artificial Mini-Enzyme

Highly Selective Indole Oxidation Catalyzed by a Mn-Containing Artificial Mini-Enzyme

Improving the catalytic performance of Pichia pastoris whole-cell biocatalysts by fermentation process

Design of Artificial Enzymes: Insights into Protein Scaffolds

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