ДВУХДОМЕННЫЕ БАКТЕРИАЛЬНЫЕ ЛАККАЗЫ: МОДИФИКАЦИЯ И ИММОБИЛИЗАЦИЯ ДЛЯ РАЗРАБОТКИ БИОЭЛЕКТРОКАТАЛИТИЧЕСКИХ СИСТЕМ

1. Komori H., Higuchi Y. Structure and molecular evolution of multicopper blue proteins. // Biomol Concepts. 2010, 1; 1(1) : 31- 40. doi: 10.1515/bmc.2010.004. PMID: 25961983.

2. Ihssen J. et al. Biochemical properties and yields of diverse bacterial laccase-like multicopper oxidases expressed in Escherichia coli //Scientific reports. -2015. -Т. 5. -№. 1. -С. 1-13.

3. Trubitsina L.I. et al. Expression of thermophilic two-domain laccase from Catenuloplanes japonicus in Escherichia coli and its activity against triarylmethane and azo dyes // РееrJ. -2021. -Т.

4. Bollella P., Katz E. Enzyme-based biosensors: Tackling electron transfer issues // Sensors. -2020. -Т. 20. -№. 12. -С. 3517

5. Akanda M.R. et al. Recent advances in nanomaterial-modified pencil graphite electrodes for electroanalysis // Electroanalysis - 2016 -V. 28 -№. 3 -P. 408-424.

6. Gunne, M., et al., Structural and redox properties of the small laccase Ssl1 from Streptomyces sviceus. // Febs j, 2014. 281(18): p. 4307-18

7. Trubitsina, L.I., et al., Structural and functional characterization of two-domain laccase from Streptomyces viridochromogenes. // Biochimie, 2015. 112: p. 151-159

8. Upadhyay, P., et al. Bioprospecting and biotechnological applications of fungal laccase. // 3 Biotech, 2016. 6(1): p. 15

9. Dey, B. and T. Dutta, Laccases: Thriving the domain of bio-electrocatalysis. // Bioelectrochemistry, 2022. 146: p. 108144

10. Olbrich AC, Schild JN, Urlacher VB. Correlation between the Т1 copper reductionpotential and catalytic activity of a small laccase. // J Inorg Biochem. 2019; 201:110843. doi: 10.1016/j.jinorgbio.2019.110843. Epub 2019 Sep 9. PMID:31536948.

11. Toscano MD, De Maria L, Lobedanz S, Ostergaard LH. Optimization of a small laccase by active-site redesign. // Chembiochem. 2013 Jul 8; 14(10) : 1209-11. doi: 10.1002/cbic.201300256. Epub 2013 Jun 14.

12. Trubitsina LI, et al. A Novel Two-Domain Laccase with Middle Redox Potential: Physicochemical and Structural Properties. // Biochemistry (Mosc). 2023; 88(10) : 1658-1667. doi: 10.1134/S0006297923100188. PMID: 38105031.

13. Abdullatypov A. et al. Functionalization of МWСNТs for Bioelectrocatalysis by Bacterial Two-Domain Laccase from Catenuloplanes japonicus. // Nanomaterials (Basel). 2023 Nov 25; 13(23) : 3019. doi: 10.3390/nаnо13233019.

14. A. Ben Tahar, K. Żelechowska, J.F. Biernat, E. Paluszkiewicz, P. Cinquin, D. Martin, A. Zebda. High catalytic performance of laccase wired to naphthylated multiwall carbon nanotubes. // BIOSENSORS & BIOELECTRONICS, 2020, V. 151, 11196

15. Aleksejeva, O. et al., Electrochemistry of a high redox potential laccase obtained by computer-guided mutagenesis combined with directed evolution. Electrochemistry Communications, 2019. 106: p. 106511

16. Milton, R.D. and S.D. Minteer, Direct enzymatic bioelectrocatalysis: differentiating between myth and reality. Journal of The Royal Society Interface, 2017. 14(131): p. 20170253