Metal ligand aromatic cation-pi interactions in metalloproteins: Ligands coordinated to metal interact with aromatic residues
Abstract
Cation-se interactions between aromatic residues and cationic amino groups in side chains and have been recognized as noncovalent bonding interactions relevant for molecular recognition and for stabilization and definition of the native structure of proteins. We propose a novel type of cation-x interaction in metalloproteins; namely interaction between ligands coordinated to a metal cation-which gain positive charge from the metal-and aromatic groups in amino acid side chains. Investigation of crystal structures of metalloproteins in the Protein Data Bank (PDB) has revealed that there exist quite a number of metalloproteins in which aromatic rings of phenylalanine, tyrosine, and tryptophan are situated close to a metal center interacting with coordinated ligands. Among these ligands are amino acids such as asparagine, aspartate, glutamate, histidine, and threonine, but also water and substrates like ethanol. These interactions play a role in the stability and conformation of metallopro...teins, and in some cases may also be directly involved in the mechanism of enzymatic reactions, which occur at the metal center. For the enzyme superoxide dismutase, we used quantum chemical computation to calculate that Trp163 has an interaction energy of 10.09 kcal mol(-1) with the ligands coordinated to iron.
Keywords:
amino acids / density functional calculations / metal complexes / metalloproteins / pi interactionsSource:
Chemistry. A European Journal, 2000, 6, 21, 3935-3942Publisher:
- Wiley-V C H Verlag Gmbh, Berlin
DOI: 10.1002/1521-3765(20001103)6:21<3935::aid-chem3935>3.0.co;2-j
ISSN: 0947-6539
PubMed: 11126954
WoS: 000165340300019
Scopus: 2-s2.0-0034602095
Collections
Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Zarić, Snežana D. AU - Popovic, DM AU - Knapp, EW PY - 2000 UR - https://cherry.chem.bg.ac.rs/handle/123456789/443 AB - Cation-se interactions between aromatic residues and cationic amino groups in side chains and have been recognized as noncovalent bonding interactions relevant for molecular recognition and for stabilization and definition of the native structure of proteins. We propose a novel type of cation-x interaction in metalloproteins; namely interaction between ligands coordinated to a metal cation-which gain positive charge from the metal-and aromatic groups in amino acid side chains. Investigation of crystal structures of metalloproteins in the Protein Data Bank (PDB) has revealed that there exist quite a number of metalloproteins in which aromatic rings of phenylalanine, tyrosine, and tryptophan are situated close to a metal center interacting with coordinated ligands. Among these ligands are amino acids such as asparagine, aspartate, glutamate, histidine, and threonine, but also water and substrates like ethanol. These interactions play a role in the stability and conformation of metalloproteins, and in some cases may also be directly involved in the mechanism of enzymatic reactions, which occur at the metal center. For the enzyme superoxide dismutase, we used quantum chemical computation to calculate that Trp163 has an interaction energy of 10.09 kcal mol(-1) with the ligands coordinated to iron. PB - Wiley-V C H Verlag Gmbh, Berlin T2 - Chemistry. A European Journal T1 - Metal ligand aromatic cation-pi interactions in metalloproteins: Ligands coordinated to metal interact with aromatic residues VL - 6 IS - 21 SP - 3935 EP - 3942 DO - 10.1002/1521-3765(20001103)6:21<3935::aid-chem3935>3.0.co;2-j ER -
@article{ author = "Zarić, Snežana D. and Popovic, DM and Knapp, EW", year = "2000", abstract = "Cation-se interactions between aromatic residues and cationic amino groups in side chains and have been recognized as noncovalent bonding interactions relevant for molecular recognition and for stabilization and definition of the native structure of proteins. We propose a novel type of cation-x interaction in metalloproteins; namely interaction between ligands coordinated to a metal cation-which gain positive charge from the metal-and aromatic groups in amino acid side chains. Investigation of crystal structures of metalloproteins in the Protein Data Bank (PDB) has revealed that there exist quite a number of metalloproteins in which aromatic rings of phenylalanine, tyrosine, and tryptophan are situated close to a metal center interacting with coordinated ligands. Among these ligands are amino acids such as asparagine, aspartate, glutamate, histidine, and threonine, but also water and substrates like ethanol. These interactions play a role in the stability and conformation of metalloproteins, and in some cases may also be directly involved in the mechanism of enzymatic reactions, which occur at the metal center. For the enzyme superoxide dismutase, we used quantum chemical computation to calculate that Trp163 has an interaction energy of 10.09 kcal mol(-1) with the ligands coordinated to iron.", publisher = "Wiley-V C H Verlag Gmbh, Berlin", journal = "Chemistry. A European Journal", title = "Metal ligand aromatic cation-pi interactions in metalloproteins: Ligands coordinated to metal interact with aromatic residues", volume = "6", number = "21", pages = "3935-3942", doi = "10.1002/1521-3765(20001103)6:21<3935::aid-chem3935>3.0.co;2-j" }
Zarić, S. D., Popovic, D.,& Knapp, E.. (2000). Metal ligand aromatic cation-pi interactions in metalloproteins: Ligands coordinated to metal interact with aromatic residues. in Chemistry. A European Journal Wiley-V C H Verlag Gmbh, Berlin., 6(21), 3935-3942. https://doi.org/10.1002/1521-3765(20001103)6:21<3935::aid-chem3935>3.0.co;2-j
Zarić SD, Popovic D, Knapp E. Metal ligand aromatic cation-pi interactions in metalloproteins: Ligands coordinated to metal interact with aromatic residues. in Chemistry. A European Journal. 2000;6(21):3935-3942. doi:10.1002/1521-3765(20001103)6:21<3935::aid-chem3935>3.0.co;2-j .
Zarić, Snežana D., Popovic, DM, Knapp, EW, "Metal ligand aromatic cation-pi interactions in metalloproteins: Ligands coordinated to metal interact with aromatic residues" in Chemistry. A European Journal, 6, no. 21 (2000):3935-3942, https://doi.org/10.1002/1521-3765(20001103)6:21<3935::aid-chem3935>3.0.co;2-j . .