Cited by 29Mitochondrial Function and PathologyEnzyme Structure and FunctionProtein Structure and Dynamics

Conformation‐specific crosslinking of mitochondrial complex I

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Ciano, Margherita, Fuszard, Matthew, Heide, Heinrich, Botting, Catherine H., Galkin, Alexander·2013·FEBS Letters

Abstract

ND3 and NDUFA9 physically interact by cross‐linking study (View interaction)

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Crossref · 10.1016/j.febslet.2013.02.039

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  • Cys39 of ND3 has been shown to become exposed under hypoxia or lack of NADH that result in low complex I activity due to the active-deactive transition.

    “Notably, one of these, Cys39 of the ND3 subunit, has been shown to become exposed under conditions of hypoxia or lack of NADH that result in low complex I activity due to the active-deactive transition26–28.”

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Authors
Ciano, M., Fuszard, M., Heide, H., Botting, C. H., & Galkin, A.
Affiliations
  • Queen's University Belfast (GB)
  • University of St Andrews (GB)
  • Goethe University Frankfurt (DE)
Corresponding author
Galkin, Alexander
Venue
FEBS Letters
Publisher
Wiley
Published
2013-02-27
Volume
587
Issue
7
Pages
867-872
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2038748296
Cited by
29
References
40
Citations by year
2025: 1 · 2024: 1 · 2022: 1 · 2021: 2 · 2019: 1 · 2018: 4 · 2017: 3 · 2016: 5 · 2015: 3 · 2014: 4 · 2013: 4
FWCI
2.39
Type
journal article
Language
en
Locations
  • FEBS Letters (publishedVersion)
  • PubMed (publishedVersion)
  • Research Portal (Queen's University Belfast) (submittedVersion)
  • INFM-OAR (INFN Catania) (submittedVersion, other-oa)
  • Zenodo (CERN European Organization for Nuclear Research) (cc-by)
Funders
  • MRC (Grant G1100051)
  • Deutsche Forschungsgemeinschaft
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
mitochondrial complex I, conformational change, NDUFA9, crosslinking, electron transport chain, coenzyme Q10, energy transduction
MeSH terms
Amino Acid Sequence, Animals, Cattle, Cross-Linking Reagents, Cysteine, Electron Transport, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Protein Conformation, Mass Spectrometry, Substrate Specificity, Succinimides, Ubiquinone, Protein Structure, Tertiary, Protein Subunits, Mitochondrial Proteins, Electron Transport Complex I, Hydrophobic and Hydrophilic Interactions

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