Cited by 17Photosynthetic Processes and MechanismsMitochondrial Function and PathologyATP Synthase and ATPases Research

Mutations at the Qo Site of the Cytochrome bc1 Complex Strongly Affect Oxygen Binding

Husen, Peter, Solov’yov, Ilia A.·2017·The Journal of Physical Chemistry B

Abstract

The homodimeric bc 1 protein complex is embedded in membranes of mitochondria and photosynthetic bacteria, where it transports protons across the membrane to maintain an electrostatic potential used to drive ATP synthesis as part of the respiratory or photosynthetic pathways. The reaction cycle of the bc 1 complex is driven by series of redox processes involving substrate molecules from the membrane, but occasional side reactions between an intermediate semiquinone substrate and molecular oxygen are suspected to be a source of toxic superoxide, which is believed to be a factor in aging. The present investigation employs molecular dynamics simulations to study the effect of mutations in the Q o binding sites of the bc 1 complex on the ability of oxygen molecules to migrate to and bind at various locations within the complex. It is found that the mutations strongly affect the ability of oxygen to bind at the Q o sites, and moreover, different behavior of the two monomers of the bc 1 complex is observed. The conformational differences at the Q o sites of the two monomers are studied in detail and discussed. The anionic form of semiquinone was identified as leading to the greatest opportunity for side reactions with oxygen.

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Crossref · 10.1021/acs.jpcb.6b08226

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49 of 49 references verified0 citation errors · 0 not checkable

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  • A leading theory of bird migration suggests that birds utilise the earth's magnetic field as a guiding tool by means of the radical pair mechanism.

    “A leading theory of bird migration suggests that birds utilise the earth's magnetic field as a guiding tool by means of the radical pair mechanism [159][160][161] .”

    From Quantum effects in the brain: A review (2020) · cites this paper as [160]

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Authors
Husen, P., & Solov’yov, I. A.
Affiliations
University of Southern Denmark (DK)
Corresponding author
  • Husen, Peter
  • Solov’yov, Ilia A.
Venue
The Journal of Physical Chemistry B
Published
2016-11-02
Volume
121
Issue
15
Pages
3308-3317
ISSN
  • 1520-5207 (ISSN-L)
  • 1520-6106
OpenAlex
W2536311932
Cited by
17
References
49
Citations by year
2024: 2 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 2 · 2016: 2
FWCI
1.56
Type
journal article
Language
en
Open access
closed
Locations
  • The Journal of Physical Chemistry B (publishedVersion)
  • PubMed (publishedVersion)
  • University of Southern Denmark Research Portal (University of Southern Denmark) (submittedVersion)
Funders
  • Russian Science Foundation (14-12-00342)
  • Danish e-Infrastructure Cooperation
  • Lundbeckfonden
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
cytochrome bc1 complex, Qo site, oxygen binding, site-directed mutations, semiquinone, superoxide, mitochondrial respiratory chain, photosynthetic electron transport, conformational differences, molecular dynamics simulation, aging
MeSH terms
Binding Sites, Mutation, Oxygen, Electron Transport Complex III, Molecular Dynamics Simulation

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