Conformation‐specific crosslinking of mitochondrial complex I
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ND3 and NDUFA9 physically interact by cross‐linking study (View interaction)
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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.”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [27]
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Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I
Chouchani, E. T., Methner, C., Nadtochiy, S. M., Logan, A., Pell, V. R., Ding, S., James, A. M., Cochemé, H. M., Reinhold, J., Lilley, K. S., et al. (2013) · Nature Medicine · doi:10.1038/nm.3212 · Cited by 619 · see citing works
- 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
- Open access
- Licence
- 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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