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Promoting laccase activity towards non-phenolic substrates: a mechanistic investigation with some laccase–mediator systems
Abstract
The oxidation of benzyl alcohols with the enzyme laccase, under mediation by appropriate mediator compounds, yields carbonylic products, whereas laccase can not oxidise these non-phenolic substrates directly. The oxidation step is performed by the oxidised form of the mediator (Med(ox)), generated on its interaction with laccase. The Med(ox) can follow either an electron transfer (ET) or a radical hydrogen atom transfer (HAT) route of oxidation of the substrates. Experimental evidence is reported that enables unambiguous assessment of the occurrence of either one the oxidation routes with each of the investigated mediators, namely, ABTS, HBT, HPI and VLA. Support to the conclusions is provided by (i) investigating the intermolecular selectivity of oxidation with appropriate substrates, (ii) attempting Hammett correlations for the oxidation of a series of 4-X-substituted benzyl alcohols, (iii) measuring the kinetic isotope effect, (iv) investigating the product pattern with suitable probe precursors. Based on these points, a HAT mechanism results to be followed by the laccase-HBT, laccase-HPI and laccase-VLA systems, whereas an ET route appears feasible in the case of the laccase-ABTS system.
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Cited by
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Engineering and Applications of fungal laccases for organic synthesis
Kunamneni, A., Camarero, S., García-Burgos, C., Plou, F. J., Ballesteros, A., & Alcalde, M. (2008) · Microbial Cell Factories · doi:10.1186/1475-2859-7-32 · Cited by 340
Bilal, M., Ashraf, S. S., Barceló, D., & Iqbal, H. M. N. (2019) · Science of The Total Environment · doi:10.1016/j.scitotenv.2019.07.224 · Cited by 239
Ashe, B., Nguyen, L. N., Hai, F. I., Lee, D.-J., van de Merwe, J. P., Leusch, F. D. L., Price, W. E., & Nghiem, L. D. (2016) · International Biodeterioration & Biodegradation · doi:10.1016/j.ibiod.2016.04.027 · Cited by 133
Laccase-catalyzed degradation of perfluorooctanoic acid
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Metadata
- Authors
- Baiocco, P., Barreca, A. M., Fabbrini, M., Galli, C., & Gentili, P.
- Venue
- Org. Biomol. Chem.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2003
- Volume
- 1
- Issue
- 1
- Pages
- 191-197
- ISSN
- 1477-0520 (ISSN-L)
- 1477-0539
- OpenAlex
- W2163000706
- Cited by
- 280
- References
- 0
- FWCI
- 9.00
- Type
- journal article
- Language
- en
- Open access
- closed
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- Baiocco, P., Barreca, A. M., Fabbrini, M., Galli, C., & Gentili, P. (2003). Promoting laccase activity towards non-phenolic substrates: a mechanistic investigation with some laccase–mediator systems. Org. Biomol. Chem. https://doi.org/10.1039/b208951c
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