Green and efficient biosynthesis of indigo from indole by engineered myoglobins

Liu, Can; Xu, Jiakun; Gao, Shu‐Qin; He, Bo; Wei, Chuan‐Wan; Wang, Xiaojuan; Wang, Zhonghua; Lin, Ying‐Wu

doi:10.1039/c8ra07825d

Cited by 24 publications

(31 citation statements)

References 33 publications

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“…The stabilization of the structure was achieved and a bathochromic shift from 535.88 to 632.44 nm (+96.56nm) in the theoretical electronic UV-visible spectra in gas phase was observed (see Figure S3). On the other hand, a similar behavior was found by Liu et al [38] , were the synthesis of indigo was achieved through the oxidation of indole by the use of H2O2 and a protein catalyst named as F34Y Mb. In this case, the in-situ synthesis was followed by UV-visible spectroscopy, by considering the appearance of a band at 670 nm assigned to the formed indigo.…”

Section: Analysis Of the Coloured Samplesupporting

confidence: 76%

“…The most significant bands are listed in Table 2. No bands associated with anhydrous, hydrated or aqueous dithionite residues were observed in the SERS experiments of leuco-indigo [38,39]. In general, the SERS spectrum of leuco-indigo is dominated by bands of medium and strong relative intensity at 551, 859, 949, 1010, 1103, 1193, 1338, 1571 and 1612 cm -1 (Figure 7C).…”

Section: Analysis Of the Coloured Samplementioning

confidence: 92%

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Identification of Coexisting Indigo Species in an Ancient Green Thread Using Direct Plasmon-Enhanced Raman Spectroscopy

Célis

Tirapegui

García

et al. 2020

J. Chil. Chem. Soc.

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A green ancient thread sample from a Chilean mummy turban was analyzed by plasmon-enhanced Raman scattering spectroscopy using a direct drop-colloidal method. The enhanced-Raman signals in the sample are associated with biomolecules from the thread and two coexisting dyes, indigo and leuco-indigo. The presence of indigo (blue colour) was identified from its most characteristic vibrational bands. Leuco-indigo (yellow colour) was identified for the first time in an ancient textile; its SERS signals are coincident with the SERS bands of a synthesized leuco-indigo. The interconversion leuco-indigo to indigo was followed by UV-visible spectroscopy. Based on theoretical calculations it is proposed that the interconversion involves a  electron delocalization mainly around the NC-CN bridge. The mixture of both dyes (indigo and leuco-indigo) is the responsible for the green colour observed.

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Section: Analysis Of the Coloured Samplesupporting

confidence: 76%

Section: Analysis Of the Coloured Samplementioning

confidence: 92%

Identification of Coexisting Indigo Species in an Ancient Green Thread Using Direct Plasmon-Enhanced Raman Spectroscopy

Célis

Tirapegui

García

et al. 2020

J. Chil. Chem. Soc.

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“…The enzymatic oxidation products of GGE were monitored by Ultra Performance Liquid Chromatography (UPLC) ESI-MS. At first, the reaction mixtures (2 mL) contained 2.5 mM of GGE dissolved in 50% ethanol (v/v), 2.0 mM H 2 O 2 , and 5.0 µM F43Y/T67R Mb in potassium phosphate buffer (pH 5.5). After reaction for 1 h, aliquots were withdrawn and diluted in acetonitrile (1:1 ratio), and then analyzed in a Waters ACQUITY UPLC/Xevo G2 QTOF system, using a reverse-phase C-18 column (ACQUITY UPLC R BEH C18 1.7 µm, 2.1 mm × 50 mm) with a precolumn at 40 • C and a flow rate of 0.5 mL/min (Liu et al, 2018). The column was further equilibrated with the mobile phase of 70% water (eluent A)/30% acetonitrile (eluent B) for 5 min.…”

Section: Product Analysis By Uplc-esi-msmentioning

confidence: 99%

Biotransformation of Lignin by an Artificial Heme Enzyme Designed in Myoglobin With a Covalently Linked Heme Group

Guo

Liu

et al. 2021

Front. Bioeng. Biotechnol.

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The conversion of Kraft lignin in plant biomass into renewable chemicals, aiming at harvesting aromatic compounds, is a challenge process in biorefinery. Comparing to the traditional chemical methods, enzymatic catalysis provides a gentle way for the degradation of lignin. Alternative to natural enzymes, artificial enzymes have been received much attention for potential applications. We herein achieved the biodegradation of Kraft lignin using an artificial peroxidase rationally designed in myoglobin (Mb), F43Y/T67R Mb, with a covalently linked heme cofactor. The artificial enzyme of F43Y/T67R Mb has improved catalytic efficiencies at mild acidic pH for phenolic and aromatic amine substrates, including Kraft lignin and the model lignin dimer guaiacylglycerol-β-guaiacyl ether (GGE). We proposed a possible catalytic mechanism for the biotransformation of lignin catalyzed by the enzyme, based on the results of kinetic UV-Vis studies and UPLC-ESI-MS analysis, as well as molecular modeling studies. With the advantages of F43Y/T67R Mb, such as the high-yield by overexpression in E. coli cells and the enhanced protein stability, this study suggests that the artificial enzyme has potential applications in the biodegradation of lignin to provide sustainable bioresource.

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“…Note that in the absence of the proximal Tyr (Ser112 or Phe112), only 1e − /1H + chemistry was observed, which suggests that the secondary sphere interactions, as provided by the redox active Tyr residue, are critical for fine-tuning the multi-e − /multi-H + reactivity for the artificial enzyme [123]. Note that the introduction ofa redox active residue such as Tyr and Trp in the heme distal pocketor on the protein surface was also shown to fine-tune the reactivity of artificial peroxidases designed in the protein scaffold of myoglobin [46,124,125].…”

Section: Artificial Metalloenzymes With Metal Clusters For Catalysismentioning

confidence: 99%

Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters

Lin

2019

Molecules

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Metalloproteins and metalloenzymes play important roles in biological systems by using the limited metal ions, complexes, and clusters that are associated with the protein matrix. The design of artificial metalloproteins and metalloenzymes not only reveals the structure and function relationship of natural proteins, but also enables the synthesis of artificial proteins and enzymes with improved properties and functions. Acknowledging the progress in rational design from single to multiple active sites, this review focuses on recent achievements in the design of artificial metalloproteins and metalloenzymes with metal clusters, including zinc clusters, cadmium clusters, iron–sulfur clusters, and copper–sulfur clusters, as well as noble metal clusters and others. These metal clusters were designed in both native and de novo protein scaffolds for structural roles, electron transfer, or catalysis. Some synthetic metal clusters as functional models of native enzymes are also discussed. These achievements provide valuable insights for deep understanding of the natural proteins and enzymes, and practical clues for the further design of artificial enzymes with functions comparable or even beyond those of natural counterparts.

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Green and efficient biosynthesis of indigo from indole by engineered myoglobins

Abstract: Myoglobin (Mb) was redesigned to a green and efficient biocatalysts for the biosynthesis of indigo from indole, exhibiting improved yield, catalytic efficiency and chemoselectivity (as high as ∼80%).

Cited by 24 publications

References 33 publications

Identification of Coexisting Indigo Species in an Ancient Green Thread Using Direct Plasmon-Enhanced Raman Spectroscopy

Identification of Coexisting Indigo Species in an Ancient Green Thread Using Direct Plasmon-Enhanced Raman Spectroscopy

Biotransformation of Lignin by an Artificial Heme Enzyme Designed in Myoglobin With a Covalently Linked Heme Group

Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters

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