2022
DOI: 10.1016/j.copbio.2021.06.022
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Cytochromes P450 in the biocatalytic valorization of lignin

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Cited by 21 publications
(15 citation statements)
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“…Aromatic O -demethylation, hydroxylation, and decarboxylation are generally considered to be rate-limiting steps in the process of conversion of lignin-derived aromatics by microorganisms ( Perez et al, 2021 ). To date, two typical oxidative enzymes related to aromatic O -demethylation, that is, cytochrome P450s (P450s) and Rieske non-heme iron oxygenases (ROs), have been found to catalyze the conversion of guaiacol and 3- O -methyl-catechol to catechol, which is the key step in the lignin degradation process mediated by microorganisms ( Bleem et al, 2022 ; Wolf et al, 2022 ). In this study, gene-LUX28_RS05610 (Rieske 2Fe-2S iron–sulfur protein YhfW) and gene-LUX28_RS04020 (CYPD_BACSU Probable bifunctional P-450/NADPH-P450 reductase 1) were downregulated in group C, while gene-LUX28_RS01310 (4-hydroxyphenylacetate 3-monooxygenase) and gene-LUX28_RS05685 (aromatic compound monooxygenase YhjG), which are considered to be catalysts for lignin-derived phenol hydroxylation ( Sucharitakul et al, 2005 ), were upregulated ( Figure 7 ).…”
Section: Resultsmentioning
confidence: 99%
“…Aromatic O -demethylation, hydroxylation, and decarboxylation are generally considered to be rate-limiting steps in the process of conversion of lignin-derived aromatics by microorganisms ( Perez et al, 2021 ). To date, two typical oxidative enzymes related to aromatic O -demethylation, that is, cytochrome P450s (P450s) and Rieske non-heme iron oxygenases (ROs), have been found to catalyze the conversion of guaiacol and 3- O -methyl-catechol to catechol, which is the key step in the lignin degradation process mediated by microorganisms ( Bleem et al, 2022 ; Wolf et al, 2022 ). In this study, gene-LUX28_RS05610 (Rieske 2Fe-2S iron–sulfur protein YhfW) and gene-LUX28_RS04020 (CYPD_BACSU Probable bifunctional P-450/NADPH-P450 reductase 1) were downregulated in group C, while gene-LUX28_RS01310 (4-hydroxyphenylacetate 3-monooxygenase) and gene-LUX28_RS05685 (aromatic compound monooxygenase YhjG), which are considered to be catalysts for lignin-derived phenol hydroxylation ( Sucharitakul et al, 2005 ), were upregulated ( Figure 7 ).…”
Section: Resultsmentioning
confidence: 99%
“…2 ). CYPs belong to this Xenobiotics metabolism category and are primarily associated with diverse metabolic activities such as inheritance transfer, drug metabolism, carbohydrate metabolism, and physiological metabolism in microorganisms [ [31] , [32] , [33] , [34] ]. Usually, bacteria are essential in the breakdown of polyphenolic compounds, for example, Sphingomonas paucimobilis SYK-6 can degrade lignin-related derivatives via the protocatechuate 4,5-cleavage pathway or multiple 3- O -methylgallate catabolic pathways [ 35 ].…”
Section: Resultsmentioning
confidence: 99%
“…Recently, researchers have been developing more effective LDAEs to accelerate the degradation of lignin. For example, the newly discovered heme-thiolate haloperoxidases 23,88,96,97 and lytic polysaccharide monooxygenases (LPMOs) are also being explored for their potential roles in the depolymerization of lignin. 9 With the identication and characterization of more ligninolytic enzymes, the mechanism of lignin depolymerization is being gradually unraveled.…”
Section: Extracellular Lignin Depolymerizationmentioning
confidence: 99%