The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Abstract
Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.
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“We modeled the location of ND3 Cys39 using structures of prokaryotic complex I (refs. 32–34). This modeling led to an orthologous mammalian core structure containing ND3 Cys39 (Fig. 3f,g and Supplementary Figs. 14 and 15).”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [32]
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Metadata
- Authors
- Sazanov, L. A., & Hinchliffe, P.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Sazanov, Leonid A.
- Venue
- Science
- Published
- 2006-03-10
- Volume
- 311
- Issue
- 5766
- Pages
- 1430-1436
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1983737836
- Cited by
- 763
- References
- 49
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 28 · 2023: 14 · 2022: 20 · 2021: 22 · 2020: 26 · 2019: 24 · 2018: 29 · 2017: 28 · 2016: 35 · 2015: 34 · 2014: 41 · 2013: 51 · 2012: 60
- FWCI
- 40.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitochondrial complex I, NADH dehydrogenase, Thermus thermophilus, hydrophilic domains, iron-sulfur clusters, flavin mononucleotide, electron transfer, frataxin, crystal structure, enzyme evolution
- MeSH terms
- Frataxin, Animals, Bacterial Proteins, Binding Sites, Oxidation-Reduction, Protein Conformation, Thermus thermophilus, Protein Structure, Tertiary, Protein Folding, Crystallography, X-Ray, Protein Subunits, Iron-Binding Proteins, Electron Transport Complex I
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