TY  - JOUR
AU  - Popovic, DM
AU  - Zarić, Snežana D.
AU  - Rabenstein, B
AU  - Knapp, EW
PY  - 2001
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/459
AB  - We generated atomic coordinates of an artificial protein that was recently synthesized to model the central part of the native cytochrome b (Cb) subunit consisting of a four-helix bundle with two hemes. Since no X-ray structure is available, the structural elements of the artificial Cb were assembled from scratch using all known chemical and structural information available and avoiding strain as much as possible. Molecular dynamics (MD) simulations applied to this model protein exhibited root-mean-square deviations as small as those obtained from MD simulations starting with the crystal structure of the native Cb subunit. This demonstrates that the modeled structure of the artificial Cb is relatively rigid and strain-free. The model structure of the artificial Cb was used to determine the redox potentials of the two hemes by calculating the electrostatic energies from the solution of the linearized Poisson-Boltzmann equation (LPBE). The calculated redox potentials agree within 20 meV with the experimentally measured values. The dependence of the redox potentials of the hemes on the protein environment was analyzed. Accordingly, the total shift in the redox potentials is mainly due to the low dielectric medium of the protein, the protein backbone charges, and the salt bridges formed between the arginines and the propionic acid groups of the hemes. The difference in the shift of the redox potentials is due to the interactions with the hydrophilic side chains and the salt bridges formed with the propionic acids of the hemes. For comparison and to test the computational procedure, the redox potentials of the two hemes in the native Cb from the cytochrome bc(1) (Cbc(1)) complex were also calculated. Also in this case the computed redox potentials agree well with experiments.
PB  - Amer Chemical Soc, Washington
T2  - Journal of the American Chemical Society
T1  - Artificial cytochrome b: Computer modeling and evaluation of redox potentials
VL  - 123
IS  - 25
SP  - 6040
EP  - 6053
DO  - 10.1021/ja003878z
ER  - 

@article{
author = "Popovic, DM and Zarić, Snežana D. and Rabenstein, B and Knapp, EW",
year = "2001",
abstract = "We generated atomic coordinates of an artificial protein that was recently synthesized to model the central part of the native cytochrome b (Cb) subunit consisting of a four-helix bundle with two hemes. Since no X-ray structure is available, the structural elements of the artificial Cb were assembled from scratch using all known chemical and structural information available and avoiding strain as much as possible. Molecular dynamics (MD) simulations applied to this model protein exhibited root-mean-square deviations as small as those obtained from MD simulations starting with the crystal structure of the native Cb subunit. This demonstrates that the modeled structure of the artificial Cb is relatively rigid and strain-free. The model structure of the artificial Cb was used to determine the redox potentials of the two hemes by calculating the electrostatic energies from the solution of the linearized Poisson-Boltzmann equation (LPBE). The calculated redox potentials agree within 20 meV with the experimentally measured values. The dependence of the redox potentials of the hemes on the protein environment was analyzed. Accordingly, the total shift in the redox potentials is mainly due to the low dielectric medium of the protein, the protein backbone charges, and the salt bridges formed between the arginines and the propionic acid groups of the hemes. The difference in the shift of the redox potentials is due to the interactions with the hydrophilic side chains and the salt bridges formed with the propionic acids of the hemes. For comparison and to test the computational procedure, the redox potentials of the two hemes in the native Cb from the cytochrome bc(1) (Cbc(1)) complex were also calculated. Also in this case the computed redox potentials agree well with experiments.",
publisher = "Amer Chemical Soc, Washington",
journal = "Journal of the American Chemical Society",
title = "Artificial cytochrome b: Computer modeling and evaluation of redox potentials",
volume = "123",
number = "25",
pages = "6040-6053",
doi = "10.1021/ja003878z"
}

Popovic, D., Zarić, S. D., Rabenstein, B.,& Knapp, E.. (2001). Artificial cytochrome b: Computer modeling and evaluation of redox potentials. in Journal of the American Chemical Society
Amer Chemical Soc, Washington., 123(25), 6040-6053.
https://doi.org/10.1021/ja003878z

Popovic D, Zarić SD, Rabenstein B, Knapp E. Artificial cytochrome b: Computer modeling and evaluation of redox potentials. in Journal of the American Chemical Society. 2001;123(25):6040-6053.
doi:10.1021/ja003878z .

Popovic, DM, Zarić, Snežana D., Rabenstein, B, Knapp, EW, "Artificial cytochrome b: Computer modeling and evaluation of redox potentials" in Journal of the American Chemical Society, 123, no. 25 (2001):6040-6053,
https://doi.org/10.1021/ja003878z . .