π-π interactions in structural stability: Role in superoxide dismutases
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In the present work, the influences of π–π interactions in superoxide
dismutase (SOD) active centers were analyzed. The majority of the aromatic
residues are involved in π–π interactions. Predominant type of interacting pairs is
His–His and His–Trp pairs. In addition to π–π interactions, π residues also form πnetworks in SOD proteins. The π–π interactions are most favorable at the pair
distance range of 5–7 Å. We observed that most of the π–π interactions shows
stabilization energies in the range −4.2 to −12.6 kJ mol-1
, while the metal assisted
π–π interactions showed an energy in the range −83.7 to −334.7 kJ mol-1
. Most of
the π–π interacting residues were evolutionary conserved and thus probably
important in maintaining the structural stability of proteins through these
interactions. A high percentage of these residues could be considered as
stabilization centers, contributing to the net stability of SOD proteins.
Keywords:
superoxide dismutase / dispersive forces / catalytic siteSource:
Journal of the Serbian Chemical Society, 2023, 88, 3, 223-235Publisher:
- Belgrade : Serbian Chemical Society
Funding / projects:
- Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM) (RS-200026)
- Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 200168 (University of Belgrade, Faculty of Chemistry) (RS-200168)
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stojanović, Srđan AU - Zlatović, Mario PY - 2023 UR - http://cherry.chem.bg.ac.rs/handle/123456789/5873 AB - In the present work, the influences of π–π interactions in superoxide dismutase (SOD) active centers were analyzed. The majority of the aromatic residues are involved in π–π interactions. Predominant type of interacting pairs is His–His and His–Trp pairs. In addition to π–π interactions, π residues also form πnetworks in SOD proteins. The π–π interactions are most favorable at the pair distance range of 5–7 Å. We observed that most of the π–π interactions shows stabilization energies in the range −4.2 to −12.6 kJ mol-1 , while the metal assisted π–π interactions showed an energy in the range −83.7 to −334.7 kJ mol-1 . Most of the π–π interacting residues were evolutionary conserved and thus probably important in maintaining the structural stability of proteins through these interactions. A high percentage of these residues could be considered as stabilization centers, contributing to the net stability of SOD proteins. PB - Belgrade : Serbian Chemical Society T2 - Journal of the Serbian Chemical Society T1 - π-π interactions in structural stability: Role in superoxide dismutases VL - 88 IS - 3 SP - 223 EP - 235 DO - 10.2298/JSC220404052S ER -
@article{ author = "Stojanović, Srđan and Zlatović, Mario", year = "2023", abstract = "In the present work, the influences of π–π interactions in superoxide dismutase (SOD) active centers were analyzed. The majority of the aromatic residues are involved in π–π interactions. Predominant type of interacting pairs is His–His and His–Trp pairs. In addition to π–π interactions, π residues also form πnetworks in SOD proteins. The π–π interactions are most favorable at the pair distance range of 5–7 Å. We observed that most of the π–π interactions shows stabilization energies in the range −4.2 to −12.6 kJ mol-1 , while the metal assisted π–π interactions showed an energy in the range −83.7 to −334.7 kJ mol-1 . Most of the π–π interacting residues were evolutionary conserved and thus probably important in maintaining the structural stability of proteins through these interactions. A high percentage of these residues could be considered as stabilization centers, contributing to the net stability of SOD proteins.", publisher = "Belgrade : Serbian Chemical Society", journal = "Journal of the Serbian Chemical Society", title = "π-π interactions in structural stability: Role in superoxide dismutases", volume = "88", number = "3", pages = "223-235", doi = "10.2298/JSC220404052S" }
Stojanović, S.,& Zlatović, M.. (2023). π-π interactions in structural stability: Role in superoxide dismutases. in Journal of the Serbian Chemical Society Belgrade : Serbian Chemical Society., 88(3), 223-235. https://doi.org/10.2298/JSC220404052S
Stojanović S, Zlatović M. π-π interactions in structural stability: Role in superoxide dismutases. in Journal of the Serbian Chemical Society. 2023;88(3):223-235. doi:10.2298/JSC220404052S .
Stojanović, Srđan, Zlatović, Mario, "π-π interactions in structural stability: Role in superoxide dismutases" in Journal of the Serbian Chemical Society, 88, no. 3 (2023):223-235, https://doi.org/10.2298/JSC220404052S . .