Investigations on the role of cation–pi interactions in active centres of superoxide dismutase
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In this study, we have analysed the influence of cation–π interactions on stability and properties of superoxide dismutase (SOD) active centres. The number of interactions formed by arginine is higher than by lysine in the cationic group, while those formed by histidine are comparatively higher in the π group. The energy contribution resulting from most frequent cation–π interactions was in the lower range of strong hydrogen bonds. The cation–π interactions involving transition metal ions as cation have energy more negative than –418.4 kJ mol-1. The stabilization centres for these proteins showed that all the residues involved in cation–π interactions were important in locating one or more of such centres. The majority of the residues involved in cation–p interactions were evolutionarily conserved and might have a significant contribution towards the stability of SOD proteins. The results presented in this work can be very useful for understanding the contribution of cation–π inter...actions to the stability of SOD active centres.
Ključne reči:
superoxide dismutase / cation–π interactions / catalytic siteIzvor:
The Journal of the Serbian Chemical Society, 2022, 87, 4, 465-477Izdavač:
- Serbian Chemical Society
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200026 (Univerzitet u Beogradu, Institut za hemiju, tehnologiju i metalurgiju - IHTM) (RS-200026)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-200168)
DOI: 10.2298/JSC220109013S
ISSN: 0352-5139
WoS: 000767372800001
Scopus: 2-s2.0-85134023973
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stojanović, Srđan Đ. AU - Zlatović, Mario PY - 2022 UR - http://cherry.chem.bg.ac.rs/handle/123456789/5507 AB - In this study, we have analysed the influence of cation–π interactions on stability and properties of superoxide dismutase (SOD) active centres. The number of interactions formed by arginine is higher than by lysine in the cationic group, while those formed by histidine are comparatively higher in the π group. The energy contribution resulting from most frequent cation–π interactions was in the lower range of strong hydrogen bonds. The cation–π interactions involving transition metal ions as cation have energy more negative than –418.4 kJ mol-1. The stabilization centres for these proteins showed that all the residues involved in cation–π interactions were important in locating one or more of such centres. The majority of the residues involved in cation–p interactions were evolutionarily conserved and might have a significant contribution towards the stability of SOD proteins. The results presented in this work can be very useful for understanding the contribution of cation–π interactions to the stability of SOD active centres. PB - Serbian Chemical Society T2 - The Journal of the Serbian Chemical Society T1 - Investigations on the role of cation–pi interactions in active centres of superoxide dismutase VL - 87 IS - 4 SP - 465 EP - 477 DO - 10.2298/JSC220109013S ER -
@article{ author = "Stojanović, Srđan Đ. and Zlatović, Mario", year = "2022", abstract = "In this study, we have analysed the influence of cation–π interactions on stability and properties of superoxide dismutase (SOD) active centres. The number of interactions formed by arginine is higher than by lysine in the cationic group, while those formed by histidine are comparatively higher in the π group. The energy contribution resulting from most frequent cation–π interactions was in the lower range of strong hydrogen bonds. The cation–π interactions involving transition metal ions as cation have energy more negative than –418.4 kJ mol-1. The stabilization centres for these proteins showed that all the residues involved in cation–π interactions were important in locating one or more of such centres. The majority of the residues involved in cation–p interactions were evolutionarily conserved and might have a significant contribution towards the stability of SOD proteins. The results presented in this work can be very useful for understanding the contribution of cation–π interactions to the stability of SOD active centres.", publisher = "Serbian Chemical Society", journal = "The Journal of the Serbian Chemical Society", title = "Investigations on the role of cation–pi interactions in active centres of superoxide dismutase", volume = "87", number = "4", pages = "465-477", doi = "10.2298/JSC220109013S" }
Stojanović, S. Đ.,& Zlatović, M.. (2022). Investigations on the role of cation–pi interactions in active centres of superoxide dismutase. in The Journal of the Serbian Chemical Society Serbian Chemical Society., 87(4), 465-477. https://doi.org/10.2298/JSC220109013S
Stojanović SĐ, Zlatović M. Investigations on the role of cation–pi interactions in active centres of superoxide dismutase. in The Journal of the Serbian Chemical Society. 2022;87(4):465-477. doi:10.2298/JSC220109013S .
Stojanović, Srđan Đ., Zlatović, Mario, "Investigations on the role of cation–pi interactions in active centres of superoxide dismutase" in The Journal of the Serbian Chemical Society, 87, no. 4 (2022):465-477, https://doi.org/10.2298/JSC220109013S . .