Freeze-fracture electron microscopy and enzyme activity of reconstituted cytochrome oxidase
Autor: | Peter Nicholls, M. Tihova, Brenda Tattrie |
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Rok vydání: | 1992 |
Předmět: | |
Zdroj: | Proceedings, annual meeting, Electron Microscopy Society of America. 50:710-711 |
ISSN: | 2690-1315 0424-8201 |
DOI: | 10.1017/s0424820100123957 |
Popis: | Eukaryotic cytochrome oxidase (CO) is a multisubunit enzyme spanning the inner mitochondrial membrane. As the terminal component in the respiratory assembly it catalyzes the reduction of oxygen to water. The size, shape and other gross features of the 3-dimensional structure of this protein have been obtained only for its 2-dimensional crystal form. The enzyme can be incorporated into liposomes of a defined lipid composition. Freeze-fracture electron microscopy of cytochrome oxidase vesicles (COV) has been combined with kinetic and spectroscopic measurements to study the phospholipid requirements for enzyme activity and protein orientation within the bilayers. |
Databáze: | OpenAIRE |
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