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Modeling the hydrogen sulfide binding to heme

Authorized Users Only
2018
Authors
Ostojić, Bojana
Schwerdtfeger, Peter
Đorđević, Dragana
Article (Published version)
Metadata
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Abstract
The binding of hydrogen sulfide to a model heme compound is investigated by coupled-cluster singles-doubles augmented by a perturbative triple excitations, CCSD(T), and density functional theory, DFT. The minimum energy path for the H2S addition to an isolated heme center of the heme protein is evaluated by adopting as a model the heme compound FeP(Im) (P = porphyrin; Im = imidazole). The FeP(Im)-H2S aduct is bound by 13.7 kcal/mol at the CCSD(T) level of theory. Relaxed potential energy curves for the lowest lying spin states of the H2S to FeP(Im) binding using DFT reveal that the binding process is associated with a "double spin-cross-over" reaction with the existence of long-distance van der Waals minima only 5-7 kcal/mol above the FeP(Im)-H2S ground state. The fact that the energy of the singlet ground state of FeP(Im)-H2S is so close in energy to the dissociation products FeP(Im) + H2S points towards the reversibility of the H2S adsorption/desorption process in biochemical reactio...ns.

Keywords:
Heme / Imidazole / H2S binding / Electronic states / Density functional theory / Coupled cluster theory
Source:
Journal of Inorganic Biochemistry, 2018, 184, 108-114
Publisher:
  • Elsevier Science Inc, New York
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-172001)
  • Modeling and Numerical Simulations of Complex Many-Body Systems (RS-171017)
Note:
  • The peer-reviewed version: https://cer.ihtm.bg.ac.rs/handle/123456789/4284

DOI: 10.1016/j.jinorgbio.2018.04.012

ISSN: 0162-0134

PubMed: 29705379

WoS: 000434493300013

Scopus: 2-s2.0-85046168618
[ Google Scholar ]
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URI
https://cer.ihtm.bg.ac.rs/handle/123456789/2286
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Ostojić, Bojana
AU  - Schwerdtfeger, Peter
AU  - Đorđević, Dragana
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2286
AB  - The binding of hydrogen sulfide to a model heme compound is investigated by coupled-cluster singles-doubles augmented by a perturbative triple excitations, CCSD(T), and density functional theory, DFT. The minimum energy path for the H2S addition to an isolated heme center of the heme protein is evaluated by adopting as a model the heme compound FeP(Im) (P = porphyrin; Im = imidazole). The FeP(Im)-H2S aduct is bound by 13.7 kcal/mol at the CCSD(T) level of theory. Relaxed potential energy curves for the lowest lying spin states of the H2S to FeP(Im) binding using DFT reveal that the binding process is associated with a "double spin-cross-over" reaction with the existence of long-distance van der Waals minima only 5-7 kcal/mol above the FeP(Im)-H2S ground state. The fact that the energy of the singlet ground state of FeP(Im)-H2S is so close in energy to the dissociation products FeP(Im) + H2S points towards the reversibility of the H2S adsorption/desorption process in biochemical reactions.
PB  - Elsevier Science Inc, New York
T2  - Journal of Inorganic Biochemistry
T1  - Modeling the hydrogen sulfide binding to heme
VL  - 184
SP  - 108
EP  - 114
DO  - 10.1016/j.jinorgbio.2018.04.012
ER  - 
@article{
author = "Ostojić, Bojana and Schwerdtfeger, Peter and Đorđević, Dragana",
year = "2018",
abstract = "The binding of hydrogen sulfide to a model heme compound is investigated by coupled-cluster singles-doubles augmented by a perturbative triple excitations, CCSD(T), and density functional theory, DFT. The minimum energy path for the H2S addition to an isolated heme center of the heme protein is evaluated by adopting as a model the heme compound FeP(Im) (P = porphyrin; Im = imidazole). The FeP(Im)-H2S aduct is bound by 13.7 kcal/mol at the CCSD(T) level of theory. Relaxed potential energy curves for the lowest lying spin states of the H2S to FeP(Im) binding using DFT reveal that the binding process is associated with a "double spin-cross-over" reaction with the existence of long-distance van der Waals minima only 5-7 kcal/mol above the FeP(Im)-H2S ground state. The fact that the energy of the singlet ground state of FeP(Im)-H2S is so close in energy to the dissociation products FeP(Im) + H2S points towards the reversibility of the H2S adsorption/desorption process in biochemical reactions.",
publisher = "Elsevier Science Inc, New York",
journal = "Journal of Inorganic Biochemistry",
title = "Modeling the hydrogen sulfide binding to heme",
volume = "184",
pages = "108-114",
doi = "10.1016/j.jinorgbio.2018.04.012"
}
Ostojić, B., Schwerdtfeger, P.,& Đorđević, D.. (2018). Modeling the hydrogen sulfide binding to heme. in Journal of Inorganic Biochemistry
Elsevier Science Inc, New York., 184, 108-114.
https://doi.org/10.1016/j.jinorgbio.2018.04.012
Ostojić B, Schwerdtfeger P, Đorđević D. Modeling the hydrogen sulfide binding to heme. in Journal of Inorganic Biochemistry. 2018;184:108-114.
doi:10.1016/j.jinorgbio.2018.04.012 .
Ostojić, Bojana, Schwerdtfeger, Peter, Đorđević, Dragana, "Modeling the hydrogen sulfide binding to heme" in Journal of Inorganic Biochemistry, 184 (2018):108-114,
https://doi.org/10.1016/j.jinorgbio.2018.04.012 . .

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