Anion-pi interactions in protein-porphyrin complexes
Abstract
In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues p...referred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.
Source:
RSC Advances, 2015, 5, 48, 38361-38372Publisher:
- Royal Soc Chemistry, Cambridge
Funding / projects:
- The study of physicochemical and biochemical processes in living environment that have impacts on pollution and the investigation of possibilities for minimizing the consequences (RS-MESTD-Basic Research (BR or ON)-172001)
- The synthesis of aminoquinoline-based antimalarials and botulinum neurotoxin A inhibitors (RS-MESTD-Basic Research (BR or ON)-172008)
DOI: 10.1039/c5ra03373j
ISSN: 2046-2069
WoS: 000353960800051
Scopus: 2-s2.0-84928914352
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Institution/Community
Fakultet veterinarske medicineTY - JOUR AU - Zlatović, Mario V. AU - Borozan, Sunčica AU - Nikolić, Milan R. AU - Stojanović, Srđan PY - 2015 UR - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1194 AB - In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes. PB - Royal Soc Chemistry, Cambridge T2 - RSC Advances T1 - Anion-pi interactions in protein-porphyrin complexes VL - 5 IS - 48 SP - 38361 EP - 38372 DO - 10.1039/c5ra03373j ER -
@article{ author = "Zlatović, Mario V. and Borozan, Sunčica and Nikolić, Milan R. and Stojanović, Srđan", year = "2015", abstract = "In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.", publisher = "Royal Soc Chemistry, Cambridge", journal = "RSC Advances", title = "Anion-pi interactions in protein-porphyrin complexes", volume = "5", number = "48", pages = "38361-38372", doi = "10.1039/c5ra03373j" }
Zlatović, M. V., Borozan, S., Nikolić, M. R.,& Stojanović, S.. (2015). Anion-pi interactions in protein-porphyrin complexes. in RSC Advances Royal Soc Chemistry, Cambridge., 5(48), 38361-38372. https://doi.org/10.1039/c5ra03373j
Zlatović MV, Borozan S, Nikolić MR, Stojanović S. Anion-pi interactions in protein-porphyrin complexes. in RSC Advances. 2015;5(48):38361-38372. doi:10.1039/c5ra03373j .
Zlatović, Mario V., Borozan, Sunčica, Nikolić, Milan R., Stojanović, Srđan, "Anion-pi interactions in protein-porphyrin complexes" in RSC Advances, 5, no. 48 (2015):38361-38372, https://doi.org/10.1039/c5ra03373j . .