Structure (London), 2004-09, Vol.12 (9), p.1645-1654
2004
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- Autor(en) / Beteiligte
- Titel
- The Oxidized Subunit B8 from Human Complex I Adopts a Thioredoxin Fold
- Ist Teil von
- Structure (London), 2004-09, Vol.12 (9), p.1645-1654
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2004
- Quelle
- ScienceDirect
- Beschreibungen/Notizen
- Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is −251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0969-2126eISSN: 1878-4186DOI: 10.1016/j.str.2004.06.021Titel-ID: cdi_proquest_miscellaneous_66837373
- Format
- –
- Schlagworte
- Amino Acid Sequence, Animals, Binding Sites, Disulfides - chemistry, Electron Transport Complex I - chemistry, Electron Transport Complex I - genetics, Electron Transport Complex I - metabolism, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits - chemistry, Protein Subunits - genetics, Protein Subunits - metabolism, Sequence Alignment, Thioredoxins - chemistry, Thioredoxins - genetics