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- W822422070 abstract "The cytochrome bc 1 complex is a multisubunit membrane protein complex, which is one of the fundamental components of the respiratory and photosynthetic electron transfer chains. The enzyme catalyzes electron transfer from ubiquinol to cytochrome c and couples this process to electrogenic translocation of protons across the membrane. The mechanism of the enzyme is known as the proton motive Q cycle. X-ray structures have been reported for the mitochondrial complex from beef and chicken and for the complex from the yeast Saccharomyces cerevisiae. These structures provided a breakthrough in understanding the enzyme mechanism and structure-function relationships. A requirement for successful 3-D crystallization of proteins is a purification procedure, which routinely provides at least 10 mg of highly purified, homogenous protein. Few basic fractionation principles have been used for the purification of the multisubunit cytochrome bc 1 complex. The traditional methods include bile salt detergent solubilization and differential ammonium sulfate precipitation hydroxyapatite chromatography with Triton X-100 as detergent or anion-exchange chromatography of dodecyl maltoside solubilized protein. This chapter describes the purification of the cytochrome bc 1 complex from the yeast Saccharomyces cerevisiae. The protocol is developed to yield a highly purified and homogeneous preparation of active enzyme suitable for 3-D crystallization. This preparation is essential for the antibody Fv fragment mediated crystallization and structure determination of the complex." @default.
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- W822422070 date "2003-01-01" @default.
- W822422070 modified "2023-10-17" @default.
- W822422070 title "Purification of the Cytochrome bc1 Complex from Yeast" @default.
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- W822422070 doi "https://doi.org/10.1016/b978-012361776-7/50012-7" @default.
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