Charge Transfer at the Qo-Site of the Cytochrome bc1 Complex Leads to Superoxide Production

Adrian Bøgh Salo, Peter Husen, Ilia A Solov'yov

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The cytochrome bc1 complex is the third protein complex in the electron transport chain of mitochondria or photosynthetic bacteria, and it serves to create an electrochemical gradient across a cellular membrane, which is used to drive ATP synthesis. The purpose of this study is to investigate interactions involving an occasionally trapped oxygen molecule (O2) at the so-called Qo site of the bc1 complex, which is one of the central active sites of the protein complex, where redox reactions are expected to occur. The investigation focuses on revealing the possibility of the oxygen molecule to influence the normal operation of the bc1 complex and acquire an extra electron, thus becoming superoxide, a biologically toxic free radical. The process is modeled by applying quantum chemical calculations to previously performed classical molecular dynamics simulations. Investigations reveal several spontaneous charge transfer modes from amino acid residues and cofactors at the Qo-site to the trapped O2 molecule.

Original languageEnglish
JournalJournal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical
Volume121
Issue number8
Pages (from-to)1771–1782
ISSN1520-6106
DOIs
Publication statusPublished - 2017

Fingerprint

inorganic peroxides
Electron Transport Complex III
cytochromes
Superoxides
Charge transfer
charge transfer
Proteins
Molecules
Oxygen
proteins
molecules
Mitochondria
mitochondria
adenosine triphosphate
Redox reactions
Poisons
Adenosinetriphosphate
oxygen
Free radicals
free radicals

Cite this

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title = "Charge Transfer at the Qo-Site of the Cytochrome bc1 Complex Leads to Superoxide Production",
abstract = "The cytochrome bc1 complex is the third protein complex in the electron transport chain of mitochondria or photosynthetic bacteria, and it serves to create an electrochemical gradient across a cellular membrane, which is used to drive ATP synthesis. The purpose of this study is to investigate interactions involving an occasionally trapped oxygen molecule (O2) at the so-called Qo site of the bc1 complex, which is one of the central active sites of the protein complex, where redox reactions are expected to occur. The investigation focuses on revealing the possibility of the oxygen molecule to influence the normal operation of the bc1 complex and acquire an extra electron, thus becoming superoxide, a biologically toxic free radical. The process is modeled by applying quantum chemical calculations to previously performed classical molecular dynamics simulations. Investigations reveal several spontaneous charge transfer modes from amino acid residues and cofactors at the Qo-site to the trapped O2 molecule.",
author = "{B{\o}gh Salo}, Adrian and Peter Husen and Solov'yov, {Ilia A}",
year = "2017",
doi = "10.1021/acs.jpcb.6b10403",
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}

Charge Transfer at the Qo-Site of the Cytochrome bc1 Complex Leads to Superoxide Production. / Bøgh Salo, Adrian; Husen, Peter; Solov'yov, Ilia A.

In: Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, Vol. 121, No. 8, 2017, p. 1771–1782.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Charge Transfer at the Qo-Site of the Cytochrome bc1 Complex Leads to Superoxide Production

AU - Bøgh Salo, Adrian

AU - Husen, Peter

AU - Solov'yov, Ilia A

PY - 2017

Y1 - 2017

N2 - The cytochrome bc1 complex is the third protein complex in the electron transport chain of mitochondria or photosynthetic bacteria, and it serves to create an electrochemical gradient across a cellular membrane, which is used to drive ATP synthesis. The purpose of this study is to investigate interactions involving an occasionally trapped oxygen molecule (O2) at the so-called Qo site of the bc1 complex, which is one of the central active sites of the protein complex, where redox reactions are expected to occur. The investigation focuses on revealing the possibility of the oxygen molecule to influence the normal operation of the bc1 complex and acquire an extra electron, thus becoming superoxide, a biologically toxic free radical. The process is modeled by applying quantum chemical calculations to previously performed classical molecular dynamics simulations. Investigations reveal several spontaneous charge transfer modes from amino acid residues and cofactors at the Qo-site to the trapped O2 molecule.

AB - The cytochrome bc1 complex is the third protein complex in the electron transport chain of mitochondria or photosynthetic bacteria, and it serves to create an electrochemical gradient across a cellular membrane, which is used to drive ATP synthesis. The purpose of this study is to investigate interactions involving an occasionally trapped oxygen molecule (O2) at the so-called Qo site of the bc1 complex, which is one of the central active sites of the protein complex, where redox reactions are expected to occur. The investigation focuses on revealing the possibility of the oxygen molecule to influence the normal operation of the bc1 complex and acquire an extra electron, thus becoming superoxide, a biologically toxic free radical. The process is modeled by applying quantum chemical calculations to previously performed classical molecular dynamics simulations. Investigations reveal several spontaneous charge transfer modes from amino acid residues and cofactors at the Qo-site to the trapped O2 molecule.

U2 - 10.1021/acs.jpcb.6b10403

DO - 10.1021/acs.jpcb.6b10403

M3 - Journal article

VL - 121

SP - 1771

EP - 1782

JO - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

JF - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

SN - 1520-6106

IS - 8

ER -