| Autor: |
Xu Z; School of Chemistry and Chemical Engineering, Guangdong Provincial Key Lab for. Green Chemical Product Technology, South China University of Technology, Guangzhou 510640, P. R. China., Zhou J; School of Chemistry and Chemical Engineering, Guangdong Provincial Key Lab for. Green Chemical Product Technology, South China University of Technology, Guangzhou 510640, P. R. China. |
| Jazyk: |
angličtina |
| Zdroj: |
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2023 Apr 25; Vol. 39 (16), pp. 5880-5890. Date of Electronic Publication: 2023 Apr 13. |
| DOI: |
10.1021/acs.langmuir.3c00343 |
| Abstrakt: |
Cellobiose dehydrogenase (CDH) is capable of direct electron transfer (DET) on electrodes and is a promising redox enzyme for bioelectrochemical applications. Its unique two-domain structure makes the function of CDH adsorbed on the surface of the electrode deeply affected by the external environment, such as ion species, strength, pH, and surface charge density. To date, however, the exact mechanism of how the external environment tailors the structure and dynamics of CDH adsorbed on the electrode surface still remains poorly understood. Here, multiscale simulations were performed to look for insight into the effect of Na + and Ca 2+ ions on the activation of CDH on oppositely charged self-assembled monolayer (NH 2 -SAM and COOH-SAM) surfaces with different surface charge densities (SCDs). Both Na + and Ca 2+ can promote CDH conformation switch from the open state to the closed state, while the promotion effect of Ca 2+ is stronger than that of Na + at the same conditions. However, the high ionic strength (IS) of Ca 2+ renders the cytochrome (CYT) domain of CDH away from the NH 2 -SAM with low SCD. In contrast, whatever the IS, the NH 2 -SAM surface with high SCD can not only enhance the CYT-surface interaction but also achieve a closed-state conformation due to a similar role of Ca 2+ . Overall, this study gains molecular-level insights into the role of ion species and surface charge in modulating the structure and conformation of CDH on the SAM surface, thereby tailoring its activity. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
