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Insights from the structure of the yeast cytochrome bc 1 complex: crystallization of membrane proteins with antibody fragments
Author(s) -
Hunte Carola
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02744-2
Subject(s) - coenzyme q – cytochrome c reductase , cytochrome c1 , chemistry , cytochrome b6f complex , oxidoreductase , electron transfer , ubiquinol , cytochrome , electron transport chain , cytochrome c , crystallography , electrochemical gradient , redox , rhodobacter sphaeroides , yeast , respiratory chain , cytochrome b , membrane , biochemistry , photochemistry , mitochondrion , photosynthesis , enzyme , organic chemistry , mitochondrial dna , gene
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.