Insights from the structure of the yeast cytochrome bc(1) complex: crystallization of membrane proteins with antibody fragments

Authors
Citation
C. Hunte, Insights from the structure of the yeast cytochrome bc(1) complex: crystallization of membrane proteins with antibody fragments, FEBS LETTER, 504(3), 2001, pp. 126-132
Citations number
44
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
504
Issue
3
Year of publication
2001
Pages
126 - 132
Database
ISI
SICI code
0014-5793(20010831)504:3<126:IFTSOT>2.0.ZU;2-C
Abstract
The ubiquinol:cytochrome c oxidoreductase (EC 1.20.2.2, QCR or cytochrome b e, complex) is a component of respiratory and photosynthetic electron trans fer chains in mitochondria and bacteria. The complex transfers electrons fr om quinol to cytochrome c. Electron transfer is coupled to proton transloca tion 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-resolutio n structure of the yeast protein reveals details of the catalytic sites of the complex, which are important for electron and proton transfer. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.