The DOI matches its Crossref record; 149 of the 149 references it cites were found in a registry or an index.
Mitochondrial Complex I
Abstract
Complex I (NADH:ubiquinone oxidoreductase) is crucial for respiration in many aerobic organisms. In mitochondria, it oxidizes NADH from the tricarboxylic acid cycle and β-oxidation, reduces ubiquinone, and transports protons across the inner membrane, contributing to the proton-motive force. It is also a major contributor to cellular production of reactive oxygen species. The redox reaction of complex I is catalyzed in the hydrophilic domain; it comprises NADH oxidation by a flavin mononucleotide, intramolecular electron transfer along a chain of iron-sulfur clusters, and ubiquinone reduction. Redox-coupled proton translocation in the membrane domain requires long-range energy transfer through the protein complex, and the molecular mechanisms that couple the redox and proton-transfer half-reactions are currently unknown. This review evaluates extant data on the mechanisms of energy transduction and superoxide production by complex I, discusses contemporary mechanistic models, and explores how mechanistic studies may contribute to understanding the roles of complex I dysfunctions in human diseases.
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Self-citationAccessory subunits are integral for assembly and function of human mitochondrial complex I
Stroud, D. A., Surgenor, E. E., Formosa, L. E., Reljic, B., Frazier, A. E., Dibley, M. G., Osellame, L. D., Stait, T., Beilharz, T. H., Thorburn, D. R., et al. (2016) · Nature · doi:10.1038/nature19754 · Cited by 600
Structure of mammalian respiratory complex I
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Self-citationMitochondria at the crossroads of health and disease
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Metadata
- Authors
- Hirst, J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2013-06-02
- Volume
- 82
- Issue
- 1
- Pages
- 551-575
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2165012926
- Cited by
- 744
- References
- 149
- FWCI
- 3.61
- Type
- journal article
- Language
- en
- Open access
- closed
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