The Role of Electrostatic Interactions in Complex Formation between Bacterial Luciferase and NADPH:FMN-oxidoreductase
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 auto...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Siberian Federal University
2018-01-01
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| Series: | Журнал Сибирского федерального университета: Серия Биология |
| Subjects: | |
| Online Access: | http://elib.sfu-kras.ru/bitstream/2311/67842/5/02_Deeva.pdf |
| Summary: | 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 |
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| ISSN: | 1997-1389 2313-5530 |