Siberian Federal University 
- Issue
- Journal of Siberian Federal University. Biology. 2018 11 (1)
- Authors
- Deeva, Anna A.; Nemtseva, Elena V.; Kratasyuk, Valentina A.
- Contact information
- Deeva, Anna A.: Siberian Federal University 79 Svobodny, Krasnoyarsk, 660041, Russia; ; Nemtseva, Elena V.: Siberian Federal University 79 Svobodny, Krasnoyarsk, 660041, Russia; Institute of BiophysicSB RAS Federal Research Center “Ks rasnoyarsk Science Center SB RAS” 50/50 Akademgorodok, Krasnoyarsk, 660036, Russia; Kratasyuk, Valentina A.: Siberian Federal University 79 Svobodny, Krasnoyarsk, 660041, Russia; Insitute of BiophysicsSB RtAS Federal Research Cen ter “Krasnoyarsk Science Center SB RAS” 50/50 Akademgorodok, Krasnoyarsk, 660036, Russia
- Keywords
- bacterial bioluminescence; luciferase; NADPH:FMN-oxidoreductase; molecular docking; protein-protein interactions; substrate transfer
- Abstract
A possible mechanism of complex formation between bacterial luciferase and NADPH:FMNoxidoreductase from Vibrio harveyi sustained by electrostatic forces is studied. The complex between the enzymes is important for a direct FMNH2 transfer without a contact with solvent, which could cause a rapid autooxidation and the formation of reactive oxygen species. In the current work the diversity of possible relative positions of NADPH:FMN-oxidoreductase and luciferase was obtained with Monte-Carlo sampling governed by oxidoreductase internal charged groups and electrostatic field caused by luciferase. Among the structures with the minimal energies, the one was found that has a proper active sites orientation for a direct FMNH2 transfer. Possible role of hydrogen bonding between Arg291 and Gln197 of luciferase and oxidoreductase, respectively, in stabilization of this complex is proposed
- Pages
- 16-29
- Paper at repository of SibFU
- https://elib.sfu-kras.ru/handle/2311/67842
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).