Cited by 765Enzyme Structure and FunctionMetalloenzymes and iron-sulfur proteinsMitochondrial Function and Pathology

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Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus

Sazanov, Leonid A., Hinchliffe, Philip·2006·Science

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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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Hydrophilic Domain of Respiratory Complex I fromThermus thermophilus
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Authors: Sazanov, L. A., & Hinchliffe, P.
Affiliations: MRC Mitochondrial Biology Unit (GB)
Corresponding author: Sazanov, Leonid A.
ORCID: Sazanov, Leonid A.
Hinchliffe, Philip
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2006-03-10
Volume: 311
Issue: 5766
Pages: 1430-1436
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1123809
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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Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus

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