Single-molecule studies of the dynamics and interactions of bacterial OXPHOS complexes
| Autor: | Mark C. Leake, Tchern Lenn |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Bioenergetic systems Bacteria Biophysics Biomolecules (q-bio.BM) Context (language use) Cell Biology Oxidative phosphorylation Computational biology Molecular Dynamics Simulation Biology Biochemistry Oxidative Phosphorylation Cell biology Bacterial protein 03 medical and health sciences 030104 developmental biology Bacterial Proteins Electron Transport Chain Complex Proteins Quantitative Biology - Biomolecules Single-particle tracking FOS: Biological sciences Fluorescent protein Function (biology) |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857:224-231 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/j.bbabio.2015.10.008 |
| Popis: | Although significant insight has been gained into biochemical, genetic and structural features of oxidative phosphorylation (OXPHOS) at the single-enzyme level, relatively little was known of how the component complexes function together in time and space until recently. Several pioneering single-molecule studies have emerged over the last decade in particular, which have illuminated our knowledge of OXPHOS, most especially on model bacterial systems. Here, we discuss these recent findings of bacterial OXPHOS, many of which generate time-resolved information of the OXPHOS machinery with the native physiological context intact. These new investigations are transforming our knowledge not only of the molecular arrangement of OXPHOS components in live bacteria, but also of the way components dynamically interact with each other in a functional state. These new discoveries have important implications towards putative supercomplex formation in bacterial OXPHOS in particular. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux. |
| Databáze: | OpenAIRE |
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