Imaging cytochrome C oxidase and FoF1-ATP synthase in mitochondrial cristae of living human cells by FLIM and superresolution microscopy
| Autor: | Ralf Mrowka, Mykhailo Ilchenko, Franziska Foertsch, Birgit Hoffmann, Ilka Starke, Michael Börsch, Christoph Biskup, Silke Noßmann, Thomas Heitkamp |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Fluorescence-lifetime imaging microscopy biology ATP synthase Cytochrome c Respiratory chain Mitochondrion 03 medical and health sciences 030104 developmental biology Enzyme chemistry biology.protein Biophysics Cytochrome c oxidase Inner mitochondrial membrane |
| Zdroj: | Single Molecule Spectroscopy and Superresolution Imaging X. |
| ISSN: | 0277-786X |
| Popis: | Cytochrome C oxidase and FoF1-ATP synthase constitute complex IV and V, respectively, of the five membrane-bound enzymes in mitochondria comprising the respiratory chain. These enzymes are located in the inner mitochondrial membrane (IMM), which exhibits large invaginations called cristae. According to recent electron cryotomography, FoF1-ATP synthases are located predominantly at the rim of the cristae, while cytochrome C oxidases are likely distributed in planar membrane areas of the cristae. Previous FLIM measurements (K. Busch and coworkers) of complex II and III unravelled differences in the local environment of the membrane enzymes in the cristae. Here, we tagged complex IV and V with mNeonGreen and investigated their mitochondrial nano-environment by FLIM and superresolution microscopy in living human cells. Different lifetimes and anisotropy values were found and will be discussed. |
| Databáze: | OpenAIRE |
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