Unraveling the Rotary Motors in FoF1-ATP Synthase by Time-Resolved Single-Molecule FRET
作者： Michael Börsch
DOI: 10.1007/978-3-319-14929-5_9
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摘要: Detection of single fluorophore molecules was reported 25 years ago, at first in a crystalline matrix cryogenic temperatures but quickly followed by single-molecule studies biological machines physiological conditions. Today, the Nobel Prize Chemistry 2014 awarded for ‘breaking resolution limit optical microscopy’, i.e. super-resolution methods that are based on active control photophysical properties fluorophores. In this chapter, development conformational analysis rotary double-motor FoF1-ATP synthase work is reviewed. Analyzing Forster resonance energy transfer (smFRET) combination with confocal fluorescence lifetime (FLIM) recording enzymes has revealed stepsize and direction two distinct coupled motor parts, reversible elastic deformations storage within protein domains, an internal mechanical regulatory mechanism to activity bacterial enzyme. TCSPC enabled duty-cycle optimized multiplexed laser excitation schemes correct smFRET data marvelous nanomachine which provides cellular currency ATP.
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