TY  - JOUR
AU  - Bozic, Bojana
AU  - Korać Jačić, Jelena
AU  - Stanković, Dalibor M.
AU  - Stanić, Marina
AU  - Romanović, Mima
AU  - Bogdanović Pristov, Jelena
AU  - Spasic, Snežana
AU  - Popovic-Bijelic, Ana
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2018
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1111
AB  - An increase in the copper pool in body fluids has been related to a number of pathological conditions, including infections. Copper ions may affect antibiotics via the formation of coordination bonds and/or redox reactions. Herein, we analyzed the interactions of Cu2+ with eight beta-lactam antibiotics using UV-Vis spectrophotometry, EPR spectroscopy, and electrochemical methods. Penicillin G did not show any detectable interactions with Cu2+. Ampicillin, amoxicillin and cephalexin formed stable colored complexes with octahedral coordination environment of Cu2+ with tetragonal distortion, and primary amine group as the site of coordinate bond formation. These beta-lactams increased the solubility of Cu2+ in the phosphate buffer. Ceftazidime and Cu2+ formed a complex with a similar geometry and gave rise to an organic radical. Ceftriaxone-Cu2+ complex appears to exhibit different geometry. All complexes showed 1: 1 stoichiometry. Cefaclor reduced Cu2+ to Cu1+ that further reacted with molecular oxygen to produce hydrogen peroxide. Finally, meropenem underwent degradation in the presence of copper. The analysis of activity against Escherichia coli and Staphylococcus aureus showed that the effects of meropenem, amoxicillin, ampicillin, and ceftriaxone were significantly hindered in the presence of copper ions. The interactions with copper ions should be taken into account regarding the problem of antibiotic resistance and in the selection of the most efficient antimicrobial therapy for patients with altered copper homeostasis.
PB  - Elsevier Science Inc, New York
T2  - Free Radical Biology and Medicine
T1  - Coordination and redox interactions of beta-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity
EP  - 285
SP  - 279
VL  - 129
DO  - 10.1016/j.freeradbiomed.2018.09.038
ER  - 

@article{
author = "Bozic, Bojana and Korać Jačić, Jelena and Stanković, Dalibor M. and Stanić, Marina and Romanović, Mima and Bogdanović Pristov, Jelena and Spasic, Snežana and Popovic-Bijelic, Ana and Spasojević, Ivan and Bajčetić, Milica",
year = "2018",
abstract = "An increase in the copper pool in body fluids has been related to a number of pathological conditions, including infections. Copper ions may affect antibiotics via the formation of coordination bonds and/or redox reactions. Herein, we analyzed the interactions of Cu2+ with eight beta-lactam antibiotics using UV-Vis spectrophotometry, EPR spectroscopy, and electrochemical methods. Penicillin G did not show any detectable interactions with Cu2+. Ampicillin, amoxicillin and cephalexin formed stable colored complexes with octahedral coordination environment of Cu2+ with tetragonal distortion, and primary amine group as the site of coordinate bond formation. These beta-lactams increased the solubility of Cu2+ in the phosphate buffer. Ceftazidime and Cu2+ formed a complex with a similar geometry and gave rise to an organic radical. Ceftriaxone-Cu2+ complex appears to exhibit different geometry. All complexes showed 1: 1 stoichiometry. Cefaclor reduced Cu2+ to Cu1+ that further reacted with molecular oxygen to produce hydrogen peroxide. Finally, meropenem underwent degradation in the presence of copper. The analysis of activity against Escherichia coli and Staphylococcus aureus showed that the effects of meropenem, amoxicillin, ampicillin, and ceftriaxone were significantly hindered in the presence of copper ions. The interactions with copper ions should be taken into account regarding the problem of antibiotic resistance and in the selection of the most efficient antimicrobial therapy for patients with altered copper homeostasis.",
publisher = "Elsevier Science Inc, New York",
journal = "Free Radical Biology and Medicine",
title = "Coordination and redox interactions of beta-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity",
pages = "285-279",
volume = "129",
doi = "10.1016/j.freeradbiomed.2018.09.038"
}

Bozic, B., Korać Jačić, J., Stanković, D. M., Stanić, M., Romanović, M., Bogdanović Pristov, J., Spasic, S., Popovic-Bijelic, A., Spasojević, I.,& Bajčetić, M.. (2018). Coordination and redox interactions of beta-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity. in Free Radical Biology and Medicine
Elsevier Science Inc, New York., 129, 279-285.
https://doi.org/10.1016/j.freeradbiomed.2018.09.038

Bozic B, Korać Jačić J, Stanković DM, Stanić M, Romanović M, Bogdanović Pristov J, Spasic S, Popovic-Bijelic A, Spasojević I, Bajčetić M. Coordination and redox interactions of beta-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity. in Free Radical Biology and Medicine. 2018;129:279-285.
doi:10.1016/j.freeradbiomed.2018.09.038 .

Bozic, Bojana, Korać Jačić, Jelena, Stanković, Dalibor M., Stanić, Marina, Romanović, Mima, Bogdanović Pristov, Jelena, Spasic, Snežana, Popovic-Bijelic, Ana, Spasojević, Ivan, Bajčetić, Milica, "Coordination and redox interactions of beta-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity" in Free Radical Biology and Medicine, 129 (2018):279-285,
https://doi.org/10.1016/j.freeradbiomed.2018.09.038 . .

TY  - JOUR
AU  - Bolic, Bojana
AU  - Mijusković, Ana
AU  - Popovic-Bijelic, Ana
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasic, Snežana
AU  - Blagojević, Duško
AU  - Spasić, Mihajlo
AU  - Spasojević, Ivan
PY  - 2015
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/846
AB  - Interactions of hydrogen sulfide (HS-/H2S), a reducing signaling species, with superoxide dimutases (SOD) are poorly understood. We applied low-T EPR spectroscopy to examine the effects of HS-/H2S and superoxide radical anion (O-2(-)) on metallocenters of FeSOD, MnSOD, and CuZnSOD. HS-/H2S did not affect FeSOD, whereas active centers of MnSOD and CuZnSOD were open to this agent. Cu2+ was reduced to Cu1+, while manganese appears to be released from MnSOD active center. Untreated and O-2(-) treated FeSOD and MnSOD predominantly show 5 d-electron systems, i.e. Fe3+ and Mn2+. Our study provides new details on the mechanisms of (patho)physiological effects of HS-/H2S.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Nitric Oxide-Biology and Chemistry
T1  - Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study
EP  - 23
SP  - 19
VL  - 51
DO  - 10.1016/j.niox.2015.09.008
ER  - 

@article{
author = "Bolic, Bojana and Mijusković, Ana and Popovic-Bijelic, Ana and Nikolić-Kokić, Aleksandra and Spasic, Snežana and Blagojević, Duško and Spasić, Mihajlo and Spasojević, Ivan",
year = "2015",
abstract = "Interactions of hydrogen sulfide (HS-/H2S), a reducing signaling species, with superoxide dimutases (SOD) are poorly understood. We applied low-T EPR spectroscopy to examine the effects of HS-/H2S and superoxide radical anion (O-2(-)) on metallocenters of FeSOD, MnSOD, and CuZnSOD. HS-/H2S did not affect FeSOD, whereas active centers of MnSOD and CuZnSOD were open to this agent. Cu2+ was reduced to Cu1+, while manganese appears to be released from MnSOD active center. Untreated and O-2(-) treated FeSOD and MnSOD predominantly show 5 d-electron systems, i.e. Fe3+ and Mn2+. Our study provides new details on the mechanisms of (patho)physiological effects of HS-/H2S.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Nitric Oxide-Biology and Chemistry",
title = "Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study",
pages = "23-19",
volume = "51",
doi = "10.1016/j.niox.2015.09.008"
}

Bolic, B., Mijusković, A., Popovic-Bijelic, A., Nikolić-Kokić, A., Spasic, S., Blagojević, D., Spasić, M.,& Spasojević, I.. (2015). Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study. in Nitric Oxide-Biology and Chemistry
Academic Press Inc Elsevier Science, San Diego., 51, 19-23.
https://doi.org/10.1016/j.niox.2015.09.008

Bolic B, Mijusković A, Popovic-Bijelic A, Nikolić-Kokić A, Spasic S, Blagojević D, Spasić M, Spasojević I. Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study. in Nitric Oxide-Biology and Chemistry. 2015;51:19-23.
doi:10.1016/j.niox.2015.09.008 .

Bolic, Bojana, Mijusković, Ana, Popovic-Bijelic, Ana, Nikolić-Kokić, Aleksandra, Spasic, Snežana, Blagojević, Duško, Spasić, Mihajlo, Spasojević, Ivan, "Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study" in Nitric Oxide-Biology and Chemistry, 51 (2015):19-23,
https://doi.org/10.1016/j.niox.2015.09.008 . .