TY  - JOUR
AU  - Zmiric, A
AU  - Milčić, Miloš K.
AU  - Zarić, Snežana D.
PY  - 2002
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/486
AB  - In this work, density functional theory calculations on geometries and energies of all possible conformers of the [Co(NH3)(6)](3+)-C6H6 cation-pi complex are described. The calculations show that stationary points are several eta(2) and the eta(3) structures. The most stable eta(3) structure has bonding energy, after basis set superposition error correction, of 32.18 kcal/mol. The energies of eta(3) structures are similar; also, the energies of 712 structures are similar while the difference in energy between eta(3) and the eta(2) structures is about 2 kcal/mol. This indicates a possibility for various orientations of the benzene ring with respect to interacting ligands in the case of metal ligand aromatic cation-pi (MLACpi) interactions and a possibility for the existence of these interactions in different molecular systems. (C) 2002 Wiley Periodicals, Inc.
PB  - John Wiley & Sons Inc, Hoboken
T2  - International Journal of Quantum Chemistry
T1  - Theoretical study of metal ligand aromatic cation-pi interactions of [Co(NH3)(6)](3+) with benzene
VL  - 87
IS  - 6
SP  - 354
EP  - 359
DO  - 10.1002/qua.10123
ER  - 

@article{
author = "Zmiric, A and Milčić, Miloš K. and Zarić, Snežana D.",
year = "2002",
abstract = "In this work, density functional theory calculations on geometries and energies of all possible conformers of the [Co(NH3)(6)](3+)-C6H6 cation-pi complex are described. The calculations show that stationary points are several eta(2) and the eta(3) structures. The most stable eta(3) structure has bonding energy, after basis set superposition error correction, of 32.18 kcal/mol. The energies of eta(3) structures are similar; also, the energies of 712 structures are similar while the difference in energy between eta(3) and the eta(2) structures is about 2 kcal/mol. This indicates a possibility for various orientations of the benzene ring with respect to interacting ligands in the case of metal ligand aromatic cation-pi (MLACpi) interactions and a possibility for the existence of these interactions in different molecular systems. (C) 2002 Wiley Periodicals, Inc.",
publisher = "John Wiley & Sons Inc, Hoboken",
journal = "International Journal of Quantum Chemistry",
title = "Theoretical study of metal ligand aromatic cation-pi interactions of [Co(NH3)(6)](3+) with benzene",
volume = "87",
number = "6",
pages = "354-359",
doi = "10.1002/qua.10123"
}

Zmiric, A., Milčić, M. K.,& Zarić, S. D.. (2002). Theoretical study of metal ligand aromatic cation-pi interactions of [Co(NH3)(6)](3+) with benzene. in International Journal of Quantum Chemistry
John Wiley & Sons Inc, Hoboken., 87(6), 354-359.
https://doi.org/10.1002/qua.10123

Zmiric A, Milčić MK, Zarić SD. Theoretical study of metal ligand aromatic cation-pi interactions of [Co(NH3)(6)](3+) with benzene. in International Journal of Quantum Chemistry. 2002;87(6):354-359.
doi:10.1002/qua.10123 .

Zmiric, A, Milčić, Miloš K., Zarić, Snežana D., "Theoretical study of metal ligand aromatic cation-pi interactions of [Co(NH3)(6)](3+) with benzene" in International Journal of Quantum Chemistry, 87, no. 6 (2002):354-359,
https://doi.org/10.1002/qua.10123 . .

TY  - JOUR
AU  - Popovic, DM
AU  - Zmiric, A
AU  - Zarić, Snežana D.
AU  - Knapp, EW
PY  - 2002
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/487
AB  - Charge separation and radical transfer in DNA photolyase from Escherichia coli is investigated by computing electrostatic free energies from a solution of the Poisson-Boltzmann equation. For the initial charge separation 450 meV are available. According to recent experiments [Aubert et al. Nature 2000, 405, 586-590] the flavin receives an electron from the proximal tryptophan W382, which consequently forms a cationic radical WH.+382. The radical state is subsequently transferred along the triad W382-W359-W306 of conserved tryptophans. The radical transfer to the intermediate tryptophan W359 is nearly isoenergetic (58 meV uphill); the radical transfer from the intermediate W359 to the distal W306 is 200 meV downhill in energy, funneling and stabilizing the radical state at W306. The resulting cationic radical WH.+306 is further stabilized by deprotonation, yielding the neutral radical W(.)306, which is 214 meV below WH.+306. The time scale of the charge recombination process yielding back the resting enzyme with FADH(.) is governed by reprotonation of W306, with a calculated lifetime of 1.2 ms that correlates well with the measured lifetime of 17 ms. In photolyase from Anacystis nidulans the radical state is partially transferred to a tyrosine [Aubert et al. Proc. Natt. Acad. Sci. U.S.A. 1999, 96, 5423-5427]. In photolyase from Escherichia coli, there is a tyrosine (Y464) close to the distal tryptophan W306 that could play this role. We show that this tyrosine cannot be involved in radical transfer, because the electron transfer from tyrosine to W306 is much too endergonic (750 meV) and a direct hydrogen transfer is likely too slow. Coupling of specific charge states of the tryptophan triad with protonation patterns of titratable residues of photolyase is small.
PB  - Amer Chemical Soc, Washington
T2  - Journal of the American Chemical Society
T1  - Energetics of radical transfer in DNA photolyase
VL  - 124
IS  - 14
SP  - 3775
EP  - 3782
DO  - 10.1021/ja016249d
ER  - 

@article{
author = "Popovic, DM and Zmiric, A and Zarić, Snežana D. and Knapp, EW",
year = "2002",
abstract = "Charge separation and radical transfer in DNA photolyase from Escherichia coli is investigated by computing electrostatic free energies from a solution of the Poisson-Boltzmann equation. For the initial charge separation 450 meV are available. According to recent experiments [Aubert et al. Nature 2000, 405, 586-590] the flavin receives an electron from the proximal tryptophan W382, which consequently forms a cationic radical WH.+382. The radical state is subsequently transferred along the triad W382-W359-W306 of conserved tryptophans. The radical transfer to the intermediate tryptophan W359 is nearly isoenergetic (58 meV uphill); the radical transfer from the intermediate W359 to the distal W306 is 200 meV downhill in energy, funneling and stabilizing the radical state at W306. The resulting cationic radical WH.+306 is further stabilized by deprotonation, yielding the neutral radical W(.)306, which is 214 meV below WH.+306. The time scale of the charge recombination process yielding back the resting enzyme with FADH(.) is governed by reprotonation of W306, with a calculated lifetime of 1.2 ms that correlates well with the measured lifetime of 17 ms. In photolyase from Anacystis nidulans the radical state is partially transferred to a tyrosine [Aubert et al. Proc. Natt. Acad. Sci. U.S.A. 1999, 96, 5423-5427]. In photolyase from Escherichia coli, there is a tyrosine (Y464) close to the distal tryptophan W306 that could play this role. We show that this tyrosine cannot be involved in radical transfer, because the electron transfer from tyrosine to W306 is much too endergonic (750 meV) and a direct hydrogen transfer is likely too slow. Coupling of specific charge states of the tryptophan triad with protonation patterns of titratable residues of photolyase is small.",
publisher = "Amer Chemical Soc, Washington",
journal = "Journal of the American Chemical Society",
title = "Energetics of radical transfer in DNA photolyase",
volume = "124",
number = "14",
pages = "3775-3782",
doi = "10.1021/ja016249d"
}

Popovic, D., Zmiric, A., Zarić, S. D.,& Knapp, E.. (2002). Energetics of radical transfer in DNA photolyase. in Journal of the American Chemical Society
Amer Chemical Soc, Washington., 124(14), 3775-3782.
https://doi.org/10.1021/ja016249d

Popovic D, Zmiric A, Zarić SD, Knapp E. Energetics of radical transfer in DNA photolyase. in Journal of the American Chemical Society. 2002;124(14):3775-3782.
doi:10.1021/ja016249d .

Popovic, DM, Zmiric, A, Zarić, Snežana D., Knapp, EW, "Energetics of radical transfer in DNA photolyase" in Journal of the American Chemical Society, 124, no. 14 (2002):3775-3782,
https://doi.org/10.1021/ja016249d . .