Three-dimensional structure of NADH: ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals
| Autor: | Kevin Leonard, Horst Haiker, Hanns Weiss |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Ubiquinol
Enzyme complex biology Neurospora crassa Electron Transfer Complex I biology.organism_classification Neurospora Mitochondria Molecular Weight chemistry.chemical_compound Electron transfer Crystallography Microscopy Electron Membrane chemistry Structural Biology Ubiquinone reductase NAD(P)H Dehydrogenase (Quinone) Electrophoresis Polyacrylamide Gel Quinone Reductases Crystallization Molecular Biology Chromatography High Pressure Liquid |
| Zdroj: | Journal of molecular biology. 194(2) |
| ISSN: | 0022-2836 |
| Popis: | NADH: ubiquinone reductase (electron transfer complex I) has been isolated from Neurospora crassa mitochondria as a monodisperse protein-phospholipid-Triton X-100 complex (1:0.04:0.15, by weight). The enzyme is in the monomeric state, has a protein molecular weight of 610,000 and consists of about 25 different subunits. Membrane crystals of the enzyme complex have been prepared by adding mixed phospholipid-Triton X-100 micelles and then removing the Triton by dialysis. Diffraction patterns of the negatively stained membrane crystals extend to about 3.9 nm, with a unit cell size of 19 nm X 38 nm and gamma = 90 degrees. The two-sided plane group packing corresponding to pgg is p22(1)2(1). By combining four sets of tilted views, a low-resolution three-dimensional structure of the protein has been calculated. The structure shows that NADH: ubiquinone reductase extends 15 nm across the membrane, projecting 9 nm from one membrane side and 1 nm from the opposite side. Only about one-third of the total protein mass is located in the membrane. The structure of NADH: ubiquinone reductase is compared with that of ubiquinol: cytochrome c reductase determined by electron microscopy of membrane crystals. |
| Databáze: | OpenAIRE |
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