Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Copyright policy )Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Mitochondrial cytochrome bc 1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc 1 complex from bovine heart reveal full views of this bifunctional enzyme. The “Rieske” iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the “Rieske” protein (subunit 9) is lodged between the two “core” subunits at the matrix side of the complex. These “core” subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized.
- Uppsala University Sweden
- University of California, Berkeley United States
- Swedish University of Agricultural Sciences Sweden
- Lawrence Berkeley National Laboratory United States
Iron-Sulfur Proteins, Models, Molecular, Binding Sites, Molecular Sequence Data, Cytochromes c1, Hydrogen Bonding, Intracellular Membranes, Crystallography, X-Ray, Cytochrome b Group, Mitochondria, Heart, Hydroquinones, Electron Transport, Electron Transport Complex III, Animals, Methacrylates, Cattle, Amino Acid Sequence, Enzyme Inhibitors, Crystallization, Oxidation-Reduction
Iron-Sulfur Proteins, Models, Molecular, Binding Sites, Molecular Sequence Data, Cytochromes c1, Hydrogen Bonding, Intracellular Membranes, Crystallography, X-Ray, Cytochrome b Group, Mitochondria, Heart, Hydroquinones, Electron Transport, Electron Transport Complex III, Animals, Methacrylates, Cattle, Amino Acid Sequence, Enzyme Inhibitors, Crystallization, Oxidation-Reduction
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