БИОЭЛЕКТРОКАТАЛИТИЧЕСКИЙ ПОТЕНЦИАЛ БАКТЕРИАЛЬНЫХ ЛАККАЗ

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

2. Mano N. and de Poulpiquet A. O2 Reduction in enzymatic biofuel cells. // Chemical Reviews, 2018. V. 118(5). P. 2392-2468.

3. Морозова О.В., Шумакович Г.П., Горбачева М.А., Шлеев С.В., Ярополов А.И. «Голубые» лакказы. // Биохимия, 2007. Т.72(10). С. 1396-1412.

4. Shleev S., Tkac J., Christenson A., Ruzgas T., Yaropolov A.I., Whittaker J.W., Gorton L. Direct electron transfer between copper-containing proteins and electrodes. // Biosensors and Bioelectronics, 2005. V.20(12). P. 2517-2554.

5. Enguita F.J., Martins L.O., Henriques A.O., Carrondo M.A. Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties. // J Biol Chem, 2003. V.278(21). P. 19416-25.

6. Chauhan P.S., Goradia B., Saxena A. Bacterial laccase: recent update on production, properties and industrial applications. // Biotech, 2017. V.7.

7. Trubitsina L.I., Tishchenko S.V., Gabdulkhakov A.G., Lisov A.V., Zakharova M.V., Leontievsky A.A. Structural and functional characterization of two-domain laccase from Streptomyces viridochromogenes. // Biochimie, 2015. V.112. V. 151-159.

8. Lisov A.V., Trubitsina L.I., Lisova Z.A., Trubitsin I.V., Zavarzina A.G., Leontievsky A.A. Transformation of humic acids by two-domain laccase from Streptomyces anulatus. // Process Biochemistry, 2019. V.76. P. 128-135.

9. Kaur R., Salwan R., Sharma V. Structural properties, genomic distribution of laccases from Streptomyces and their potential applications. // Process Biochemistry, 2022. V.11. P. 133-144.

10. Luo, Q., Chen Y., Xia J., Wang K. -Q., Cai Y. -J., Liao X. -R., Guan, Z. -B. Functional expression enhancement of Bacillus pumilus CotA-laccase mutantWLF through site-directed mutagenesis. // Enzyme and Microbial Technology, 2018. V.109. P. 11-19.

11. Trubitsina, L.I., Abdullatypov A.V., Larionova A.P., Trubitsin I.V., Alferov S.V., Ponamoreva O.N., Leontievsky A.A., Expression of thermophilic two-domain laccase from Catenuloplanes japonicus in Escherichia coli and its activity against triarylmethane and azo dyes. // PeerJ 2021. V.9. e11646.

12. Алферов, С.В., Абдуллатыпов А.В., Трубицина Л.И., Якимович С.В., Бабкина Е.Е., Петракова М.П., Понаморева О.Н. Биоэлектрокаталитические бактериальных двухдоменных лакказ. // Известия Тульского государственного университета. Естественные науки, 2022. № 1ю С. 9-20.

13. Christenson A., Shleev S., Mano N., Heller A., Gorton L. Redox potentials of the blue copper sites of bilirubin oxidases. // Biochimica et Biophysica Acta (BBA) -Bioenergetics, 2006. V.1757(12). P. 1634-1641.

14. Che A. -F., Germain V., Cretin M., Cornu D., Innocent C., Tingry S. Fabrication of free-standing electrospun carbon nanofibers as efficient electrode materials for bioelectrocatalysis. // New Journal of Chemistry, 2011. V.35(12). P. 2848-2853.

15. Torrinha, Á. ; Jiyane, N. ; Sabela, M. ; Bisetty, K. ; Montenegro, M.C.B.S.M. ; Araújo, A.N., Nanostructured pencil graphite electrodes for application as high power biocathodes in miniaturized biofuel cells and bio-batteries. // Scientific Reports 2020. V. 10(1). P.16535.