Anion-pi interactions in active centers of superoxide dismutases
Članak u časopisu (Recenzirana verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predic...ted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins. (C) 2017 Elsevier B.V. All rights reserved.
Ključne reči:
Anion-pi interactions / Superoxide dismutase / Proteins / Active centers / Interaction energyIzvor:
International Journal of Biological Macromolecules, 2018, 106, 559-568Izdavač:
- Elsevier Science Bv, Amsterdam
Finansiranje / projekti:
- Proučavanje fizičkohemijskih i biohemijskih procesa u životnoj sredini koji utiču na zagađenje i istraživanje mogućnosti za minimiziranje posledica (RS-MESTD-Basic Research (BR or ON)-172001)
- Interakcije prirodnih proizvoda, njihovih derivata i kompleksnih jedinjenja sa proteinima i nukleinskim kiselinama (RS-MESTD-Basic Research (BR or ON)-172055)
Napomena:
- This is peer-reviewed version of the following article: Ribić, V. R.; Stojanović, S. Đ.; Zlatović, M. V. Anion–π Interactions in Active Centers of Superoxide Dismutases. International Journal of Biological Macromolecules 2018, 106, 559–568. https://doi.org/10.1016/j.ijbiomac.2017.08.050
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3152
DOI: 10.1016/j.ijbiomac.2017.08.050
ISSN: 0141-8130
PubMed: 28811207
WoS: 000417661600063
Scopus: 2-s2.0-85028012582
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Ribić, Vesna R. AU - Stojanović, Srđan Đ. AU - Zlatović, Mario PY - 2018 UR - https://cherry.chem.bg.ac.rs/handle/123456789/3151 AB - We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins. (C) 2017 Elsevier B.V. All rights reserved. PB - Elsevier Science Bv, Amsterdam T2 - International Journal of Biological Macromolecules T1 - Anion-pi interactions in active centers of superoxide dismutases VL - 106 SP - 559 EP - 568 DO - 10.1016/j.ijbiomac.2017.08.050 ER -
@article{ author = "Ribić, Vesna R. and Stojanović, Srđan Đ. and Zlatović, Mario", year = "2018", abstract = "We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins. (C) 2017 Elsevier B.V. All rights reserved.", publisher = "Elsevier Science Bv, Amsterdam", journal = "International Journal of Biological Macromolecules", title = "Anion-pi interactions in active centers of superoxide dismutases", volume = "106", pages = "559-568", doi = "10.1016/j.ijbiomac.2017.08.050" }
Ribić, V. R., Stojanović, S. Đ.,& Zlatović, M.. (2018). Anion-pi interactions in active centers of superoxide dismutases. in International Journal of Biological Macromolecules Elsevier Science Bv, Amsterdam., 106, 559-568. https://doi.org/10.1016/j.ijbiomac.2017.08.050
Ribić VR, Stojanović SĐ, Zlatović M. Anion-pi interactions in active centers of superoxide dismutases. in International Journal of Biological Macromolecules. 2018;106:559-568. doi:10.1016/j.ijbiomac.2017.08.050 .
Ribić, Vesna R., Stojanović, Srđan Đ., Zlatović, Mario, "Anion-pi interactions in active centers of superoxide dismutases" in International Journal of Biological Macromolecules, 106 (2018):559-568, https://doi.org/10.1016/j.ijbiomac.2017.08.050 . .