Length of photocycle of proteorhodopsin

Value 15 msec
Organism Generic
Reference Béjà O, Aravind L, Koonin EV, Suzuki MT, Hadd A, Nguyen LP, Jovanovich SB, Gates CM, Feldman RA, Spudich JL, Spudich EN, DeLong EF. Bacterial rhodopsin: evidence for a new type of phototrophy in the sea. Science. 2000 Sep 15 289(5486):1902-6.PubMed ID10988064
Method bacterial rhodopsin was encoded in the genome of an uncultivated gamma-proteobacterium and shared highest amino acid sequence similarity with archaeal rhodopsins. The protein was functionally expressed in Escherichia coli and bound retinal to form an active, light-driven proton pump. The new rhodopsin exhibited a photochemical reaction cycle with intermediates and kinetics characteristic of archaeal proton-pumping rhodopsins.
Comments The decay of proteorhodopsin O is the rate limiting step in the photocycle and is fit well by a single exponential process of 15 msec with an upward baseline shift of 13% of the initial amplitude. A possible explanation is heterogeneity in the proteorhodopsin population, with 87% of the molecules exhibiting a 15 ms photocycle and 13% a slower recovery
Entered by Uri M
ID 103732