Insights from the structure of the yeast cytochrome bc1 complex: crystallization of membrane proteins with antibody fragments

• Published in: FEBS Letters Vol. 504; no. 3; pp. 126 - 132
• Main Author: Hunte, Carola
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier B.V 31-08-2001
• Subjects: Antibody fragment; Cell Membrane - enzymology; Complex III; Crystallization; Crystallography, X-Ray; Electron Transport; Electron Transport Complex III - chemistry; Fungal Proteins - chemistry; Lipid Bilayers - metabolism; Models, Chemical; Models, Molecular; Oxidation-Reduction; Oxidoreductase; Protein Binding; Protein Conformation; Protons; Q cycle; Quinol; Quinones - chemistry; Q cycle; Antibody fragment; Quinol; Oxidoreductase; Complex III; Crystallization
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(01)02744-2

The ubiquinol:cytochrome
c oxidoreductase (EC 1.20.2.2, QCR or cytochrome
bc
1 complex) is a component of respiratory and photosynthetic electron transfer chains in mitochondria and bacteria. The complex transfers electrons from quinol to cytochrome
c. Electron transfer is coupled to proton translocation across the lipid bilayer, thereby generating an electrochemical proton gradient, which conserves the free energy of the redox reaction. The yeast complex was crystallized with antibody Fv fragments, a promising technique to obtain well-ordered crystals from membrane proteins. The high-resolution structure of the yeast protein reveals details of the catalytic sites of the complex, which are important for electron and proton transfer.