Abstract
Bacteriorhodopsin (bR) is a seven-helix light-driven proton-pump that has been extensively studied structurally and functionally. However, the single molecule kinetics of the reaction cycle remain unknown. Here, we use HS-AFM methods to characterize the single molecule kinetics of wild-type bR exposed to continuous light and short light pulses. We monitored bR conformational changes with millisecond temporal resolution and determined that the cytoplasmic gate opens 2.9ms after photon absorption, and stays open for proton capture for 13.2 ms.
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